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Proteins are defying textbooks

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We bet this isn’t the only time they have done so. 😉

Here, from U Utah Healthcare:

Open any introductory biology textbook and one of the first things you’ll learn is that our DNA spells out the instructions for making proteins, tiny machines that do much of the work in our body’s cells. Results from a study published on Jan. 2 in Science defy textbook science, showing for the first time that the building blocks of a protein, called amino acids, can be assembled without blueprints – DNA and an intermediate template called messenger RNA (mRNA). A team of researchers has observed a case in which another protein specifies which amino acids are added.

“This surprising discovery reflects how incomplete our understanding of biology is,” says first author Peter Shen, Ph.D., a postdoctoral fellow in biochemistry at the University of Utah. “Nature is capable of more than we realize.”

To put the new finding into perspective, it might help to think of the cell as a well-run factory. Ribosomes are machines on a protein assembly line, linking together amino acids in an order specified by the genetic code. When something goes wrong, the ribosome can stall, and a quality control crew is summoned to the site. To clean up the mess, the ribosome is disassembled, the blueprint is discarded, and the partly made protein is recycled.

Yet this study reveals a surprising role for one member of the quality control team, a protein conserved from yeast to man named Rqc2. More.

But what is this about “Nature is capable of more than we realize”? Does nature have a mind that has a search space for solutions?

Like a half-made car with extra horns and wheels tacked to one end, a truncated protein with an apparently random sequence of alanines and threonines looks strange, and probably doesn’t work normally. But the nonsensical sequence likely serves specific purposes. The code could signal that the partial protein must be destroyed, or it could be part of a test to see whether the ribosome is working properly. Evidence suggests that either or both of these processes could be faulty in neurodegenerative diseases such as Alzheimer’s, Amyotrophic lateral sclerosis (ALS), or Huntington’s.

“There are many interesting implications of this work and none of them would have been possible if we didn’t follow our curiosity,” says Brandman. “The primary driver of discovery has been exploring what you see, and that’s what we did. There will never be a substitute for that.”

Are these people trying to say, don’t fire us because we find evidence for design in nature?

If so, let’s hope they are not forced to yelp some fake disclaimer at a press conference.

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Comments
Obviously you grossly misunderstood what I wrote, hence you’ve jumped into wrong conclusions that took you farther away from the main subject.
Strange. Even after reading your post #121 it seems that I perfectly well understood what you wrote.
At least AVS asked some questions before arriving at wrong conclusions, but you didn’t even try to clarify the situation before giving your opinion.
It turns out that I am actually able to read any of the questions and answers that get posted here. It is therefor irrelevant who actually asks these questions of you.
I suggest you read post #121 or simply refrain from writing ridiculously disoriented opinions on this subject.
It is a 'ridiculously disoriented' opinion that rather than collecting papers you actually learn to understand them first? Or are you claiming that you actually understand the papers perfectly well and your statement "actually I understand very little of what I read" refers to something completely different? Or maybe when you write "Apparently there is assumed knowledge that is not explicitly available to non-biologists." this does not mean that you actually lack this knowledge?
Ideally, the software should be designed, developed, tested, implemented, supported, by the same biologists. But they are busy working on difficult and time consuming research, hence don’t have any time left for other endeavors.
At least here I agree with you. That's why in all cases I know of such software is indeed always designed, developed, tested, and implemented by biologists or in close collaboration with biologists. You should take your own advice to heart rather than ignoring it. Maybe, just maybe, if it turns out that you can't find biologists to collaborate on your project you either need to put a bit more effort into finding such collaborators or you should examine if maybe this project is not of any worth to biologists (hence their reluctance to collaborate with you on this). Anyway, just some thoughts. Feel free to write them off as 'ridiculously disoriented opinions'. It's your time and you can spend it on whatever floats your boat.hrun0815
January 10, 2015
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#119 hrun0815 Obviously you grossly misunderstood what I wrote, hence you've jumped into wrong conclusions that took you farther away from the main subject. At least AVS asked some questions before arriving at wrong conclusions, but you didn't even try to clarify the situation before giving your opinion. I suggest you read post #121 or simply refrain from writing ridiculously disoriented opinions on this subject. Enjoy the weekend. :)Dionisio
January 10, 2015
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AVS, They identified Nat10 as the enzyme responsible for the cytidine acetylation, which seems like the explicit objective of that paper, according to the title and the abstract, but I did not find where they explain how Nat10 got in the picture, at the right time, in the right place, in the right amount required for the cytidine acetylation. There are several conditional statements that should be clarified for a software development project, that perhaps are not required for the paper to be understood by other biologists. Apparently there is assumed knowledge that is not explicitly available to non-biologists. Perhaps that's explained in the rest of the paper, or maybe not, that's why I highlight the statement so that I have a reminder to keep looking for those pieces that may not be explained in the paper, but somewhere else, because maybe they are obvious things assumed by the biology researchers, but unknown to the system analysts working on the programming specs. When developing software, no detail can be left out of the picture. Biologists know many things that they assume known by their colleagues who will read their papers, but software analysts, engineers, developers, don't know many things about biology, but still have to develop a software that deals with those concepts they don't know. Perhaps that's one of the reasons the concept of interdisciplinary teamwork has reached some level of acceptance in academic and research circles these days. Ideally, the software should be designed, developed, tested, implemented, supported, by the same biologists. But they are busy working on difficult and time consuming research, hence don't have any time left for other endeavors. Have you ever worked on engineering software development projects? Are you familiar with the process that precedes the actual programming? The creation of the tech documentation to write the programming specs? Again, no details should be left out. Not one. Before the programmers get to work coding the myriad of instructions that make the system, the tech specs must be precisely defined, no ambiguities are allowed, no 'maybes' or 'perhaps' or 'suppositions'. Interactive animation software development deals with the fact that the user can modify the conditions continuously, in order to test different scenarios and choreographies for every given story within a project. Hence the tech specs must consider all the possible variants, either in implicit generic terms, or in explicit lists of cases. All the objects involved in every choreography must be associated with a detailed description of the conditions that cause the object to appear on the scene, what it does, how it does it, etc. Are we starting to understand each other better now? I appreciate you have decided to engage in a serious discussion with me on this subject. Maybe you could provide the details I'm looking for, thus saving me a substantial amount of time that I could use somewhere else. :)Dionisio
January 10, 2015
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That's what I was afraid of Dio. The majority of the things you highlight "that are not explained in the given paper," are in fact explained in the paper. I'm surprised none of your "biologist" friends have pointed this out to you yet actually. You see, what happens is in most cellular biology papers a question or unsolved problem is highlighted in the abstract, and then the paper goes onto explain the answer or at least part of it. Let's take that paper I mentioned: "the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified," it waht you highlighted. The paper then goes on to specifically identify the acetyltransferase and the acetylation site. This is why part of the paper’s title is “identification of acetylation sites and the responsible acetyltransferase in fission yeast, Schizosaccharomyces pombe” This is most likely due to the fact that you don’t actually read the majority of the paper and that you certainly don’t understand what you do read. I don't know what to say Dio, but it's not looking good for you. It sounds like you are just compiling the most useless list of publications known to man.AVS
January 10, 2015
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I try and highlight some of the issues that are not explained in the given paper, but may be described in other papers or might be explained in future papers soon. This is kind of like a reminder, so that I keep an eye on the given subjects, in order to detect any information that may pop up in another paper and shed more light on some of the issues that currently are poorly described. [...] I can’t understand many things, actually I understand very little of what I read, but I try to see if the gathering method and tools work well with this ‘puzzle pieces’ finding approach. It’s like working on an extended ‘proof of concept’ task.
Have you considered that rather than putting all this work into this puzzle pieces approach it might be more useful to learn how to properly read and understand maybe a single paper you 'collect'. It seems relatively obvious that without actually understanding the papers it is going to be difficult for you to evaluate any of them. And it is not totally clear how you think you can 'detect any information that may pop up in another paper and shed more light on some of the issues that currently are poorly described' if according to your own admission you 'understand very little of what [you] read'.hrun0815
January 10, 2015
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AVS,
Why do you highlight certain statements such as “the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified?”
Ok, that's a valid question. I try and highlight some of the issues that are not explained in the given paper, but may be described in other papers or might be explained in future papers soon. This is kind of like a reminder, so that I keep an eye on the given subjects, in order to detect any information that may pop up in another paper and shed more light on some of the issues that currently are poorly described. FYI - I'm using Mind Meister + Zotero + various interconnected WordPress web logs to organize (online) the information that I'm gathering, so that I can share it with others (privately) and review it again later, with the help of a few friends who are biologists and a friend who is a scientist working on AI issues. For each specific mechanism, seen from an information-processing perspective, I try to see some of the outstanding questions and connect the related 'dots' when possible, using newer information that keeps coming in. It's like trying to complete a puzzle, where the new research papers provide the missing pieces, so everyday the puzzle is getting more complete, but then newer, more detailed puzzles may open up during the process. The references I share here are part of the references I'm gathering separately with the online tools I mentioned above. I can't understand many things, actually I understand very little of what I read, but I try to see if the gathering method and tools work well with this 'puzzle pieces' finding approach. It's like working on an extended 'proof of concept' task. In order to make things a little easier for me, I've narrowed down the area I'm more interested in now, which is related to the mechanisms for the asymmetric mitosis affecting the cell fate specification and determination. But other areas are very interesting too. In Biology many things are interesting, but I can only look into a very small fraction of the whole picture without loosing my sanity. :) These are fascinating times to watch the advance of scientific research. I'm sure we all agree on this. Every new discovery sheds more light on very interesting biological systems. Working on this is not easy for me, because I'm new in this area and know very little, even after taking online biology 101 classes offered by some universities free of charge. A parallel project includes interactive 4D animation software development, which I've started on C++/C# .NET with some XAML, using the MSVS IDE, but lately considering to do it in Xamarin and Azure environments. All this is difficult, although the most difficult part is understanding enough biology just to find the missing pieces of the puzzle and test the information-gathering method. Both, the studying and the software development issues consume a substantial part of my limited time. Some of my colleagues would have done all this much faster than I can, but they just don't feel the same attraction to biology, hence they don't want to work on this. Did I answer your question properly? Please, let me know. Thank you. PS. Did you understand what I wrote to you @112? Perhaps you will like it. It's something my classmates sometimes said to each other at the university. I don't recall anyone saying that to me, though. The original version is in the Cyrillic alphabet, but in this blog it's easier for me to write the phonetic version using the English alphabet.Dionisio
January 10, 2015
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Oh Dio. Don't worry, your posts don't bother me in the least, in fact I find them quite humorous. Some of the papers even sound interesting and I skim through them, so thank you for that! I am merely trying to help you out because I fear you have a bit of a misunderstanding as to what you think you are doing. Why do you highlight certain statements such as "the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified?" It's a pretty simple question I think, but I'll understand if you don't want to answer.AVS
January 10, 2015
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AVS, Why do you care so much about what I post or how I do it? You're not the moderator of the thread, nor the administrator of the site. If you don't like it, or it bothers you, you may ignore my posts completely. You don't have to read them. BTW, your derogatory comments are completely worthless. But at times I take the fact that my posts bother you as a tremendous compliment. :)Dionisio
January 10, 2015
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Aurelio Smith Since you took it so seriously, then why didn't you answer the question that triggered your personal attacks the way it should have been answered? Didn't you know the answer? Weren't you sure how to answer it? The only correct answer to that question is: Yes, of course it can be. The reliability of a document has nothing to do with the ethnicity or cultural background of the authors. That's a fact attested by many examples in history. That should be clear to anyone. But apparently it was not to you when you read the question. Is it now? Then, after answering it correctly, thus presenting your strong position on the subject, you could have asked any other question you would have deemed pertinent in order to clarify the subject. But that's not what you did. Why? What happened to you? Think about it.Dionisio
January 10, 2015
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Movie of the eukaryotic 40S and 60S ribosomal subunits in complex with initiation factors eIF1 and eIF6, respectively. The movie visualizes the increased complexity of the eukaryotic ribosome, compared to bacterial and archaeal ribosomes. The ribosomal rRNA conserved across all kingdoms is depicted in grey and universally conserved proteins are depicted in light blue. Protein and rRNA segments shared between eukaryotes and archaea, but not bacteria are depicted in orange, and segments exclusive to eukaryotes are depicted in red. http://www.mol.biol.ethz.ch/groups/ban_group/RibosomeDionisio
January 10, 2015
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Aurelio Smith Ty umnitsa, prosto molodets! :)Dionisio
January 10, 2015
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AVS Ty umnitsa, prosto molodets! :)Dionisio
January 10, 2015
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Or maybe just explain why you highlight things like "the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified."AVS
January 10, 2015
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Hey Dio, just a quick question, if you could answer it concisely as possible that would be great. What do you think you are accomplishing by copying and pasting the abstracts of all these papers?AVS
January 10, 2015
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A single acetylation of 18 S rRNA is essential for biogenesis of the small ribosomal subunit... doi: 10.1074/jbc.M114.593996 Biogenesis of eukaryotic ribosome is a complex event involving a number of non-ribosomal factors. http://www.ncbi.nlm.nih.gov/pubmed/25086048
Dionisio
January 10, 2015
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RNA cytidine acetyltransferase of small-subunit ribosomal RNA doi: 10.1371/journal.pone.0112156. The eukaryotic small-subunit (SSU) ribosomal RNA (rRNA) has two evolutionarily conserved acetylcytidines. However, the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified. http://www.ncbi.nlm.nih.gov/pubmed/25402480
Dionisio
January 10, 2015
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hrun0815 Ty umnitsa, prosto molodets! :) :) :)Dionisio
January 10, 2015
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Structural basis for diversity in the SAM clan of riboswitches. doi: 10.1073/pnas.1312918111 In bacteria, sulfur metabolism is regulated in part by seven known families of riboswitches that bind S-adenosyl-l-methionine (SAM). Direct binding of SAM to these mRNA regulatory elements governs a downstream secondary structural switch that communicates with the transcriptional and/or translational expression machinery. The most widely distributed SAM-binding riboswitches belong to the SAM clan, comprising three families that share a common SAM-binding core but differ radically in their peripheral architecture. Although the structure of the SAM-I member of this clan has been extensively studied, how the alternative peripheral architecture of the other families supports the common SAM-binding core remains unknown. http://www.ncbi.nlm.nih.gov/pubmed/24753586
Dionisio
January 10, 2015
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I’m Hispanic and my first language is Spanish, my question, immediately followed by a :) was obviously a joke.
Ah, yes. Because being part of a group gives license to insult the remainder of the group? I understand that you were attempting to make a joke. You failed.hrun0815
January 10, 2015
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The structure and function of the eukaryotic ribosome. doi: 10.1101/cshperspect.a011536. Structures of the bacterial ribosome have provided a framework for understanding universal mechanisms of protein synthesis. However, the eukaryotic ribosome is much larger than it is in bacteria, and its activity is fundamentally different in many key ways. Recent cryo-electron microscopy reconstructions and X-ray crystal structures of eukaryotic ribosomes and ribosomal subunits now provide an unprecedented opportunity to explore mechanisms of eukaryotic translation and its regulation in atomic detail. This review describes the X-ray crystal structures of the Tetrahymena thermophila 40S and 60S subunits and the Saccharomyces cerevisiae 80S ribosome, as well as cryo-electron microscopy reconstructions of translating yeast and plant 80S ribosomes. Mechanistic questions about translation in eukaryotes that will require additional structural insights to be resolved are also presented. http://www.ncbi.nlm.nih.gov/pubmed/22550233
Dionisio
January 10, 2015
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#101 Aurelio Smith Vamos, tranquilo amigo, no os preocupéis tanto. Éso ha sido solamente una broma. No os lo toméis tan serio. :)
Not sure whether Dionisio is making a racist slur against people of Spanish ethnicity or is ironically implying that I am racist against people of Spanish ethnicity. Either way it’s pretty despicable.
I can understand your reaction. But to those who have read my previous comments in this blog, where I have stated on several occasions that I'm Hispanic and my first language is Spanish, my question, immediately followed by a :) was obviously a joke.
I may be overly sensitive. My mother’s family were Spanish – hence Aurelio.
Well, I'm much more Hispanic than you are. Born Hispanic, from Hispanic parents, grandparents, etc. Perhaps much earlier in my genealogy tree there were other ethnicities too, because we know that some Mediterranean regions of Spain were occupied by various Middle East or North Africa ethnicities at some points in history, but I have no records of that. Now you see that no offense was intended whatsoever. It would have been like attacking my own ethnic roots. But most importantly, I strongly believe that all humans, regardless of ethnicity, cultural background, nationality, social position, anything, share the same dignity that comes from being created by the same Maker, according to the purpose of His will, for His glory. I'm not better than anybody else. However, based on what I know about myself, I'm worse than most people I know. As the apostle Paul said, I'm the chief of sinners. The good news is that God loves us (including you and me). He has graciously offered the Way to reconcile us with Him forever. Hallelujah! Espero leer tus próximos comentarios. Anímate y escribe más. Ésta es una vía, quizás un poco más amistosa y relajada, para intercambiar información y opiniones sobre interesantes temas científicos de actualidad. Os deseo un buen fin de semana. Os saludo cordialmente.Dionisio
January 10, 2015
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hrun is confused and cannot follow along. I never said that all genetically engineered splicing's result in no proteins forming. Never. Not only that hrun cannot present any evidence that amino acid sequence determines shape and function. If a gene coding for a protein that does NOT require a chaperone or chaperones to fold then it should do OK in another host. Get one that requires a chaperone or chaperones and it won't do anything in a foreign host.Joe
January 10, 2015
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#98 addendum gpuccio Your original statement, that has caused so much 'itching' to some interlocutors, was written in post #5. It's really taken too long for some interlocutors to understand it. Oh, well. Things happen. :)Dionisio
January 10, 2015
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gpuccio Your statement quoted in post #92 seems correct to me. The way you used the conjunction 'except' before a statement that indicated the only thing that was not included in or referred to by the preceding statement, seems very clear to me. For example, the statement "I don't want to drink anything, except water" is as clear as water. :) I'd suggest you refrain from discussing anything with interlocutors (specially the ones across the ocean) who may not know the correct meaning and use of certain words. :) For example, some folks in that part of the world can't tell the difference between Slovakia and Slovenia. They think that it's just that both guys 'Vakia' and 'Venia' are 'slow'. :) Besides, their disrespectful comments in this blog, although tolerated by some moderators here for unknown to me reasons*, do not motivate to engage in any kind of serious discussion with them. Perhaps the only benefit I see from your discussions is that others can read what you write. :)Dionisio
January 10, 2015
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AVS: Thank you for the comments. You are entitled to judging my communication style as you like. I will go on trying to communicate as I think is correct. However, please believe (if you want) that there was never in my mind any intention or desire to "lighten the blow in the fact that this protein creates a random sequence that adds information", for the very simple reason that, IMHO, that is not a blow at all. I see no problem at all in the fact that it is possible to add functional information by creating a random sequence in a controlled context. My only intention (believe it or not) was to clarify the differences between what happens in this context and what happens in mRNA directed protein synthesis, because at the beginning of this thread there seemed to be great confusion about that. In Italy, lawyers are not exactly considered so bad as they are in the USA, but maybe we can catch up, if we really try. :) However, I always enjoyed this old joke: A physician, an engineer, and an attorney were discussing who among them belonged to the oldest of the three professions represented. The physician said, "Remember, on the sixth day God took a rib from Adam and fashioned Eve, making him the first surgeon. Therefore, medicine is the oldest profession." The engineer replied, "But, before that, God created the heavens and earth from chaos, and thus he was the first engineer. Therefore, engineering is an older profession than medicine." Then, the lawyer spoke up. "Yes," he said, "But who do you think created chaos?"gpuccio
January 10, 2015
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Reconstitution of a minimal ribosome-associated ubiquitination pathway with purified factors. doi: 10.1016/j.molcel.2014.07.006. Ribosomes stalled on aberrant mRNAs engage quality control mechanisms that degrade the partially translated nascent polypeptide. Ubiquitination of the nascent protein is mediated by the E3 ligase Listerin via a mechanism involving ribosome subunit dissociation. Here, we reconstitute ribosome-associated ubiquitination with purified factors to define the minimal components and essential steps in this process. We find that the primary role of the ribosome splitting factors Hbs1, Pelota, and ABCE1 is to permit Listerin access to the nascent chain. Listerin alone can discriminate 60S- from 80S-nascent chain complexes to selectively ubiquitinate the former. Splitting factors can be bypassed by artificially removing the 40S subunit, suggesting that mere steric hindrance impedes Listerin recruitment. This was illustrated by a cryo-EM reconstruction of the 60S-Listerin complex that identifies a binding interface that clashes with the 40S ribosomal subunit. These results reveal the mechanistic logic of the core steps in a ribosome-associated quality control pathway. http://www.ncbi.nlm.nih.gov/pubmed/25132172
Dionisio
January 10, 2015
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Protein synthesis. Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains. doi: 10.1126/science.1259724. In Eukarya, stalled translation induces 40S dissociation and recruitment of the ribosome quality control complex (RQC) to the 60S subunit, which mediates nascent chain degradation. Here we report cryo-electron microscopy structures revealing that the RQC components Rqc2p (YPL009C/Tae2) and Ltn1p (YMR247C/Rkr1) bind to the 60S subunit at sites exposed after 40S dissociation, placing the Ltn1p RING (Really Interesting New Gene) domain near the exit channel and Rqc2p over the P-site transfer RNA (tRNA). We further demonstrate that Rqc2p recruits alanine- and threonine-charged tRNA to the A site and directs the elongation of nascent chains independently of mRNA or 40S subunits. Our work uncovers an unexpected mechanism of protein synthesis, in which a protein--not an mRNA--determines tRNA recruitment and the tagging of nascent chains with carboxy-terminal Ala and Thr extensions ("CAT tails"). http://www.ncbi.nlm.nih.gov/pubmed/25554787
Dionisio
January 10, 2015
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Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex. doi: 10.1073/pnas.1413882111 All organisms have [...] mechanisms to manage the stalling of ribosomes upon translation of aberrant mRNA. In eukaryotes, the large ribosomal subunit-associated quality control complex (RQC), composed of the listerin/Ltn1 E3 ubiquitin ligase and cofactors, mediates the ubiquitylation and extraction of ribosome-stalled nascent polypeptide chains for proteasomal degradation. How RQC recognizes stalled ribosomes and performs its functions has not been understood. Using single-particle cryoelectron microscopy, we have determined the structure of the RQC complex bound to stalled 60S ribosomal subunits. The structure establishes how Ltn1 associates with the large ribosomal subunit and properly positions its E3-catalytic RING domain to mediate nascent chain ubiquitylation. The structure also reveals that a distinguishing feature of stalled 60S particles is an exposed, nascent chain-conjugated tRNA, and that the Tae2 subunit of RQC, which facilitates Ltn1 binding, is responsible for selective recognition of stalled 60S subunits. RQC components are engaged in interactions across a large span of the 60S subunit surface, connecting the tRNA in the peptidyl transferase center to the distally located nascent chain tunnel exit. This work provides insights into a mechanism linking translation and protein degradation that targets defective proteins immediately after synthesis, while ignoring nascent chains in normally translating ribosomes. http://www.ncbi.nlm.nih.gov/pubmed/25349383
Dionisio
January 10, 2015
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Gpuc, an unbroken stretch of hydrophobic residues is absolutely required, besides that there is little similarity between signal peptides. In fact, this is what makes predicting signal sequences very difficult. You can attach any random hydrophobic sequence that is about 6-15 residues long, to a cytosolic protein and it will be transported to the ER. These studies have already been done. The alpha-helix structure thing was a guess on my part, although it doesn’t really matter whether it’s a helix, a beta-sheet, whatever; the most important thing is that it makes some kind of structure that is recognized by HSP1, which apparently it does. The absolute clearest way to say it would have been “it adds the specific information that activates the heat shock response.” I don’t see any need for the “no specific information” part unless you are trying to lighten the blow in the fact that this protein creates a random sequence that adds information. It adds specific information, so the phrase “no specific information added” should not be in the sentence. But that’s just my opinion, although I do pride myself on saying exactly what I mean and meaning exactly what I say. =) You obviously aren’t aware of the attitude toward lawyers here in the US of A, it’s not a compliment. Ever heard of the phrase “ambulance chasers” or seen Breaking Bad? And Dio, you don’t know your rear-end from a hole in the ground, so I wouldn’t try to judge the clarity of someone’s words or open my mouth at all, if I were you. =)AVS
January 9, 2015
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#91 gpuccio
“no specific information added except for a signal that means so and so” simply means that the signal information is added, and no other information. Is that doublespeak?
No. That's clearspeak. :)Dionisio
January 9, 2015
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