RNA measurements may yield less insight than assumed

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December 19, 2014

News, Origin Of Life

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Origin Of Life}

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The majority of RNA expression differences between individuals have no connection to the abundance of a corresponding protein, report scientists from the University of Chicago and Stanford University in Science on Dec. 18. The findings point to a yet-unidentified cellular mechanism that regulates gene expression and suggest studies that rely only on RNA measurements to characterize gene function require further analysis.

“The chief assumption for studies of RNA differences is that they ultimately reflect differences in an end product, which is protein,” said senior study author Yoav Gilad, PhD, professor of human genetics at the University of Chicago. “But it turns out in most cases this may not be true.”

Interesting, when we consider the high hopes placed in RNA world.

See also: Welcome to “RNA world,” the five-star hotel of origin-of-life theories

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The non-catalytic N-terminal domain of ACS7 is involved in the post-translational regulation of this gene doi: 10.1093/jxb/eru211 Post-transcriptional control of the expression of the 1-aminocyclopropane-1-carboxylate synthase (ACS) gene family is important for maintaining appropriate levels of ethylene production. However, the molecular mechanism underlying the post-transcriptional regulation of type 3 ACS proteins remains unclear. Multiple sequence alignment revealed that the N-terminus of type 3 ACSs was longer than that of other ACSs. Fusing the N-terminal 54 residues of ACS7, the sole type 3 ACS in Arabidopsis, to the ?-glucuronidase (GUS) reporter significantly decreased the stability of N7(1–54)–GUS fusion protein. Among these 54 residues, residues 1–14 conferred this negative effect on the GUS fusion gene. Consistently, a truncated form of ACS7 lacking residues 1–14 was more stable than full-length ACS7 when transgenically expressed in Arabidopsis and led to a more severe ethylene response phenotype in the light-grown transgenic seedlings. Interestingly, the ACS7 N-terminus had no effect on the stability of N7–GUS and ACS7 proteins at the etiolated seedling stage. Both exogenous 1-aminocyclopropane-1-carboxylic acid (ACC) treatment and salt stress could rescue the levels of accumulation of N7–GUS fusion protein in light-grown seedlings. These results suggest that the non-catalytic N-terminus of ACS7 is involved in its own post-translational regulation. The proteasome inhibitor MG132 suppressed degradation of full-length ACS7 in vivo, but had little effect on the N-terminal truncated form of ACS7, indicating that the N-terminus mediates the regulation of ACS7 stability through the ubiquitin–26S proteasome pathway. http://jxb.oxfordjournals.org/content/early/2014/05/24/jxb.eru211Dionisio_{December 21, 2014
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Post-translational modifications of intermediate filament proteins: mechanisms and functions doi:10.1038/nrm3753 Intermediate filaments (IFs) are cytoskeletal and nucleoskeletal structures that provide mechanical and stress-coping resilience to cells, contribute to subcellular and tissue-specific biological functions, and facilitate intracellular communication. IFs, including nuclear lamins and those in the cytoplasm (keratins, vimentin, desmin, neurofilaments and glial fibrillary acidic protein, among others), are functionally regulated by post-translational modifications (PTMs). Proteomic advances highlight the enormous complexity and regulatory potential of IF protein PTMs, which include phosphorylation, glycosylation, sumoylation, acetylation and prenylation, with novel modifications becoming increasingly appreciated. Future studies will need to characterize their on–off mechanisms, crosstalk and utility as biomarkers and targets for diseases involving the IF cytoskeleton. http://www.nature.com/nrm/journal/v15/n3/abs/nrm3753.htmlDionisio_{December 21, 2014
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The growing landscape of lysine acetylation links metabolism and cell signaling doi:10.1038/nrm3841 Lysine acetylation is a conserved protein post-translational modification that links acetyl-coenzyme A metabolism and cellular signalling. Recent advances in the identification and quantification of lysine acetylation by mass spectrometry have increased our understanding of lysine acetylation, implicating it in many biological processes through the regulation of protein interactions, activity and localization. In addition, proteins are frequently modified by other types of acylations, such as formylation, butyrylation, propionylation, succinylation, malonylation, myristoylation, glutarylation and crotonylation. The intricate link between lysine acylation and cellular metabolism has been clarified by the occurrence of several such metabolite-sensitive acylations and their selective removal by sirtuin deacylases. These emerging findings point to new functions for different lysine acylations and deacylating enzymes and also highlight the mechanisms by which acetylation regulates various cellular processes. http://www.nature.com/nrm/journal/v15/n8/abs/nrm3841.htmlDionisio_{December 21, 2014
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Non-histone protein methylation as a regulator of cellular signalling and function doi:10.1038/nrm3915 Methylation of Lys and Arg residues on non-histone proteins has emerged as a prevalent post-translational modification and as an important regulator of cellular signal transduction mediated by the MAPK, WNT, BMP, Hippo and JAK–STAT signalling pathways. Crosstalk between methylation and other types of post-translational modifications, and between histone and non-histone protein methylation frequently occurs and affects cellular functions such as chromatin remodelling, gene transcription, protein synthesis, signal transduction and DNA repair. With recent advances in proteomic techniques, in particular mass spectrometry, the stage is now set to decode the methylproteome and define its functions in health and disease. http://www.nature.com/nrm/journal/vaop/ncurrent/abs/nrm3915.htmlDionisio_{December 21, 2014
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Any outstanding questions on the OP? :)Dionisio_{December 21, 2014
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Post-translational modifications The diversity of modifications that a nascent peptide acquires as it is transported to its target cellular location is long established, as is the ability of particular tags such as phosphorylation and ubiquitylation to regulate signalling and protein turnover, respectively. But in more recent years we have seen a renaissance of interest in the ability of additional modifications — from ubiquitin-like proteins to moieties such as sugars or methyl, acetyl and prenyl groups — to target specific sites in proteins and to coordinately exert dynamic control over protein function in diverse cell biological contexts. http://www.nature.com/nrm/series/ptm/index.htmlDionisio_{December 21, 2014
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Post-translational modification of mitochondria as a novel mode of regulation. doi: 10.1016/j.exger.2014.03.006 Mitochondria not only form the metabolic hub, but also are crucial players in many cellular pathways, like apoptosis and innate immune response, putting the organelle in a central position in controlling cellular function and fate. As novel and powerful regulators of mitochondrial processes and hence mitochondrial-controlled pathways, post-translational modifications (PTMs) have emerged in the last years. In this review, we will summarize the current state of knowledge on PTMs occurring in mammalian mitochondria with a focus on phosphorylation, acetylation, succinylation and ubiquitination. We will highlight their regulatory role in metabolism, autophagy and apoptosis as well as communicating element to cellular stress response pathways such as the immune response. Finally, we will discuss open questions in this exciting research area and point out how mitochondrial PTMs might impact age-associated pathologies. http://www.ncbi.nlm.nih.gov/pubmed/24632076Dionisio_{December 21, 2014
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PTHGRN: unraveling post-translational hierarchical gene regulatory networks using PPI, ChIP-seq and gene expression data. Interactions among transcriptional factors (TFs), cofactors and other proteins or enzymes can affect transcriptional regulatory capabilities of eukaryotic organisms. Post-translational modifications (PTMs) cooperate with TFs and epigenetic alterations to constitute a hierarchical complexity in transcriptional gene regulation. While clearly implicated in biological processes, our understanding of these complex regulatory mechanisms is still limited and incomplete. Transcriptional regulation dominated by interactions between transcription factors (TFs) and DNA sequences is a center for control of gene expression in eukaryotic organisms. The ability of TFs to regulate the target genes is largely modified by post-translational modifications (PTMs) among TFs, cofactors and other proteins or enzymes upstream of transcriptional process. The combinational action of PTMs, TFs, as well as epigenetic factors forms a hierarchical “regime” to perform gene regulation. Many biological processes or functions like human disease, cell differentiation and development involve the synergistic coordination of these multi-level regulators. Despite its importance, our understanding of such complex regulatory mechanisms is incomplete. https://globalmedicaldiscovery.com/key-medical-diagnostics-articles/pthgrn-unraveling-post-translational-hierarchical-gene-regulatory-networks-using-ppi-chip-seq-gene-expression-data/Dionisio_{December 21, 2014
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A conserved type IV pilin signal peptide H-domain is critical for the post-translational regulation of flagella-dependent motility DOI: 10.1111/mmi.12673 This novel post-translational regulatory mechanism, which employs components that promote biofilm formation to inhibit motility, can provide a rapid response to changing environmental conditions. A model for this regulatory mechanism, which may also be present in other prokaryotes, is discussed. http://onlinelibrary.wiley.com/doi/10.1111/mmi.12673/abstractDionisio_{December 21, 2014
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Post-transcriptional and post-translational regulation of epithelial transport Although defective epithelial fluid and electrolyte transport can lead to a range of debilitating conditions, including cystic fibrosis, diabetes insipidus, and diarrhoeal diseases, we are only beginning to understand the molecular mechanisms involved. While the gene expression profiles of different epithelial cell populations are important in determining their compliment of transport proteins, it is the post-transcriptional and post-translational regulatory machinery that ultimately dictates their transporting phenotype. This symposium will highlight recent advances in this rapidly evolving field of epithelial physiology by highlighting how post-transcriptional and post-translational regulatory mechanisms dynamically regulate fluid and electrolyte transport in health and disease. http://www.physiology2014.org/scientific-programme/symposia/post-transcriptional-and-post-translational-regulation-epithelialDionisio_{December 21, 2014
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New insights into extracellular and post-translational regulation of TGF-? family signalling pathways doi: 10.1093/jb/mvt046. Members of the transforming growth factor-? (TGF-?) family of secreted proteins are present in all multicellular animals. TGF-? proteins are versatile intercellular signalling molecules that orchestrate cell fate decisions during development and maintain homeostasis in adults. The Smad family of signal transducers implements TGF-? signals in responsive cells. Given the ability of TGF-? ligands to induce dramatic responses in target cells, numerous regulatory mechanisms exist to prevent unintended consequences. Here we review new reports of extracellular and post-translational regulation in Drosophila and vertebrates. Extracellular topics include the regulation of TGF-? signalling range and the coordination between tissue morphogenesis and TGF-? signalling. Post-translational topics include the regulation of TGF-? signal transduction by Gsk3-? phosphorylation of Smads and by cycles of Smad mono- and deubiquitylation. Extension of the ubiquitylation data to the Hippo pathway is also discussed. http://www.ncbi.nlm.nih.gov/pubmed/23698094Dionisio_{December 21, 2014
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#17 bornagain77 Excellent! That's it. Thank you.Dionisio_{December 21, 2014
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#16 addendum The ability to self-renew indefinitely and differentiate into all cells of the body makes human pluripotent stem cells (hPSCs), including human embryonic stem cells (hESCs) and induced pluripotent stem cells (hiPSCs), valuable for research and clinical applications that require specific cell types. Although recent studies have greatly advanced our understanding of cellular pluripotency and its potential utility, it is still unclear how these cells establish, maintain and modulate their pluripotency during cellular reprogramming and differentiation. Recent evidence indicates that the complex signaling networks involved in the regulation of cellular pluripotency are tightly controlled through multiple mechanisms, including post-translational modifications (PTMs). PTMs diversify and extend protein function beyond what is dictated by gene transcripts. They reversibly or irreversibly alter the structure and properties of proteins through biochemical reactions, and a variety of PTMs allow eukaryotic cells to dynamically regulate their signal integration and physiological states. As analytical approaches have improved, the biological influences of many types of PTMs have been identified and are routinely analyzed in many systems. The importance of PTMs is known historically because of their effects on the enzymatic activity of kinases1 and protein degradation. Based on previous and emerging data, it seems evident that PTMs are involved in regulating almost all cellular events, including gene expression, signal transduction, protein-protein interaction, cell-cell interaction, and communication between the intracellular and extracellular environment. Therefore, perturbation of PTMs in cells frequently affects cell physiology as a whole. In addition, the alteration of cellular states (e.g., differentiation of hPSCs or malignant transformation of primary cells) may be accompanied by acquisition of unique PTM hallmarks. http://www.nature.com/cr/journal/v24/n2/full/cr2013151a.htmlDionisio_{December 21, 2014
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Dionisio, although I don't know what the exact nuances of this particular finding are, of an additional level of regulation for genes/proteins, I do know of a finding for gene/protein regulation that blows neo-Darwinian precepts out of the water. A little known fact, a fact that is very antagonistic to the genetic reductionism model of neo-Darwinism, is that, besides environmental factors, even our thoughts and feelings can 'epigenetically' control the gene expression of our bodies:
Scientists Finally Show How Your Thoughts Can Cause Specific Molecular Changes To Your Genes, - December 10, 2013 Excerpt: “To the best of our knowledge, this is the first paper that shows rapid alterations in gene expression within subjects associated with mindfulness meditation practice,” says study author Richard J. Davidson, founder of the Center for Investigating Healthy Minds and the William James and Vilas Professor of Psychology and Psychiatry at the University of Wisconsin-Madison. “Most interestingly, the changes were observed in genes that are the current targets of anti-inflammatory and analgesic drugs,” says Perla Kaliman, first author of the article and a researcher at the Institute of Biomedical Research of Barcelona, Spain (IIBB-CSIC-IDIBAPS), where the molecular analyses were conducted.,,, the researchers say, there was no difference in the tested genes between the two groups of people at the start of the study. The observed effects were seen only in the meditators following mindfulness practice. In addition, several other DNA-modifying genes showed no differences between groups, suggesting that the mindfulness practice specifically affected certain regulatory pathways. http://www.tunedbody.com/scientists-finally-show-thoughts-can-cause-specific-molecular-changes-genes/ Networks of Genes Respond to Social Experiences - October 13, 2013 Excerpt: It is subjective mind and perception that changes genes, not just external situations. http://jonlieffmd.com/blog/networks-of-genes-respond-to-social-experiences Controlling genes with your thoughts - November 11, 2014 Excerpt: “For the first time, we have been able to tap into human brainwaves, transfer them wirelessly to a gene network and regulate the expression of a gene depending on the type of thought. Being able to control gene expression via the power of thought is a dream that we’ve been chasing for over a decade,” says Fussenegger. http://www.sciencedaily.com/releases/2014/11/141111111317.htm Study shows clear new evidence for mind-body connection - Mindfulness-based cancer recovery - Nov. 3, 2014 Excerpt: A group,, has demonstrated that telomeres – protein complexes at the end of chromosomes – maintain their length in breast cancer survivors who practise meditation or are involved in support groups, while they shorten in a comparison group without any intervention. Although the disease-regulating properties of telomeres aren't fully understood, shortened telomeres are associated with several disease states, as well as cell aging, while longer telomeres are thought to be protective against disease. "We already know that psychosocial interventions like mindfulness meditation will help you feel better mentally, but now for the first time we have evidence that they can also influence key aspects of your biology," http://m.medicalxpress.com/news/2014-11-evidence-mind-body.html
That 'mind' can have a pronounced effect on gene expression is simply completely antithetical to the 'bottom up' reductive materialism upon which neo-Darwinism is based. A view that entails that we are merely victims of our genes with no control whatsoever. Of related note, focused attention of the mind, besides having a pronounced effect on gene expression, is now also shown to have a pronounced effect on 'brain plasticity':
The Case for the Soul - InspiringPhilosophy - (4:03 minute mark, Brain Plasticity including Schwartz's work) - Oct. 2014 - video The Mind is able to modify the brain. Moreover, Idealism explains all anomalous evidence of personality changes due to brain injury, whereas physicalism does not explain mind. https://www.youtube.com/watch?v=oBsI_ay8K70
Quote:
“You don’t have a soul. You are a soul. You have a body.” George MacDonald - Annals of a Quiet Neighborhood - 1892
Verse and Music:
Mark 12:30 Love the Lord your God with all your heart and with all your soul and with all your mind and with all your strength.' CMA Country Christmas 2014 | Michael W. Smith & Carrie Underwood - "All Is Well" https://www.youtube.com/watch?v=cjZfeEJgNRw
bornagain77_{December 21, 2014
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Protein post-translational modifications and regulation of pluripotency in human stem cells doi:10.1038/cr.2013.151 Post-translational modifications (PTMs) are known to be essential mechanisms used by eukaryotic cells to diversify their protein functions and dynamically coordinate their signaling networks. Defects in PTMs have been linked to numerous developmental disorders and human diseases, highlighting the importance of PTMs in maintaining normal cellular states. Human pluripotent stem cells (hPSCs), including embryonic stem cells (hESCs) and induced pluripotent stem cells (hiPSCs), are capable of self-renewal and differentiation into a variety of functional somatic cells; these cells hold a great promise for the advancement of biomedical research and clinical therapy. The mechanisms underlying cellular pluripotency in human cells have been extensively explored in the past decade. In addition to the vast amount of knowledge obtained from the genetic and transcriptional research in hPSCs, there is a rapidly growing interest in the stem cell biology field to examine pluripotency at the protein and PTM level. This review addresses recent progress toward understanding the role of PTMs (glycosylation, phosphorylation, acetylation and methylation) in the regulation of cellular pluripotency. http://www.nature.com/cr/journal/v24/n2/full/cr2013151a.htmlDionisio_{December 21, 2014
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#13 BA77 Thank you.Dionisio_{December 21, 2014
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#12 Box FYI - an important rule in the ethical code of blog discussions is that you should refrain from asking any kind of easy questions that might force your interlocutors to admit they don't know. Violating such basic rule might lead to unfair treatment or humiliation of your interlocutors, which is politically incorrect, hence unacceptable. Now you know for next time. :)Dionisio_{December 21, 2014
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Dionisio, I will take a look over it in a bit and see if I have anything in my notes to addbornagain77_{December 21, 2014
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hrun0815: These results do not suggest that there is an unidentified mechanism of gene regulation. Translational regulation and protein stability has been described and studied for over 25 years.
And is there any clarity yet? What regulates genes? Sure there has been the identification of a multitude of "influencers" which are in turn influenced and so forth. But where in this web of interactions is a regulator? To put it another way: what has decision power? Are we really expecting to find the "decision-molecule"? Is such a concept even thinkable?Box_{December 21, 2014
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News, Please, don't take me wrong, I'm not trying to put at end to the discussion here. Just trying to comment on the interesting OP. :)Dionisio_{December 21, 2014
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BA77, Please, give me a hand with this. I don't want to shutdown this discussion. That's not my intention. :)Dionisio_{December 21, 2014
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Another related paper: Regulation of autophagy by protein post-translational modification doi:10.1038/labinvest.2014.131 Autophagy is a lysosome-mediated intracellular protein degradation process that involves about 38 autophagy-related genes as well as key signaling pathways that sense cellular metabolic and redox status, and has an important role in quality control of macromolecules and organelles. As with other major cellular pathways, autophagy proteins are subjected to regulatory post-translational modification. Phosphorylation is so far the most intensively studied post-translational modification in the autophagy process, followed by ubiquitination and acetylation. An interesting and new area is also now emerging, which appears to complement these more traditional mechanisms, and includes O-GlcNAcylation and redox regulation at thiol residues. Identification of the full spectrum of post-translational modifications of autophagy proteins, and determination of their impact on autophagy will be crucial for a better understanding of autophagy regulation, its deficits in diseases, and how to exploit this process for disease therapies. http://www.nature.com/labinvest/journal/vaop/ncurrent/full/labinvest2014131a.htmlDionisio_{December 21, 2014
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Any questions yet? :)Dionisio_{December 21, 2014
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Another related paper: Post-translational dual regulation of cytochrome P450 aromatase at the catalytic and protein levels by phosphorylation/dephosphorylation DOI: 10.1111/febs.13021 The post-translational regulation of aromatase has not been well characterized as compared with transcriptional regulation. Several studies of post-translational regulation have focused on decreases in catalytic activity following phosphorylation. We report here dual post-translational regulation of aromatase, at the catalytic activity and protein levels. Microsomal aromatase prepared from JEG-3 cells was rapidly inactivated and subsequently degraded in the presence of a cytosolic fraction with calcium, magnesium, and ATP. In a reconstituted system consisting of microsomal and cytosolic fractions, aromatase was protected from protein degradation by treatment with alkaline phosphatase, whereas degradation was enhanced by treatment with calcineurin inhibitors (FK506 and cyclosporin A). Furthermore, aromatase was protected from degradation by treatment with kinase inhibitors, especially the calcium/calmodulin kinase inhibitors KN62 and KN93. Similarly to the reconstituted system, aromatase in cultured JEG-3 cells was protected from degradation by KN93, whereas FK503 increased degradation in the presence of cycloheximide, although cellular aromatase mRNA levels were unchanged by these reagents. Knockdown of calcineurin and calcium/calmodulin kinase II (CaMKII) with small interfering RNAs resulted in a dose-dependent increase in aromatase degradation and protection from degradation, respectively. The cytosol fraction-dependent phosphorylation of microsomal aromatase was inhibited by calcineurin, KN62, and KN93, and promoted by CaMKII and FK506. These results indicate that aromatase is regulated acutely at the catalytic activity level and subsequently at the enzyme content level by CaMKII/calcineurin-dependent phosphorylation/dephosphorylation. http://onlinelibrary.wiley.com/doi/10.1111/febs.13021/abstractDionisio_{December 21, 2014
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Another related article: Three novel quantitative trait loci for skin thickness in swine identified by linkage and genome-wide association studies DOI: 10.1111/age.12163 Skin is the largest organ in the pig body and plays a key role in protecting the body against pathogens and excessive water loss. Deciphering the genetic basis of swine skin thickness would enrich our knowledge about the skin. To identify the loci for porcine skin thickness, we first performed a genome scan with 194 microsatellite markers in a White Duroc × Erhualian F2 intercross. We identified three genome-wide significant QTL on pig chromosomes (SSC) 4, 7 and 15 using linkage analysis. The most significant QTL was found on SSC7 with a small confidence interval of ~5 cM, explaining 23.9 percent of phenotypic variance. Further, we conducted a genome-wide association study (GWAS) using Illumina PorcineSNP60 Beadchips for the F2 pedigree and a population of Chinese Sutai pigs. We confirmed significant QTL in the F2 pedigree and replicated QTL on SSC15 in Chinese Sutai pigs. A meta-analysis of GWASs on both populations detected a genomic region associated with skin thickness on SSC4. GWAS results were generally consistent with QTL mapping. Identical-by-descent analysis defined QTL on SSC7 in a 683-kb region harboring an interesting candidate gene: HMGA1. On SSC15, the linkage disequilibrium analysis showed a haplotype block of 2.20 Mb that likely harbors the gene responsible for skin thickness. Our findings provide novel insights into the genetic basis of swine skin thickness, which would benefit further understanding of porcine skin function. http://onlinelibrary.wiley.com/doi/10.1111/age.12163/abstractDionisio_{December 21, 2014
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Quick explanation of terminology
Quantitative trait locus http://en.wikipedia.org/wiki/Quantitative_trait_locus Expression quantitative trait loci http://en.wikipedia.org/wiki/Expression_quantitative_trait_loci
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Is this the abstract of the original paper?
Impact of regulatory variation from RNA to protein DOI: 10.1126/science.1260793 Alexis Battle1,2,*,‡, Zia Khan3,†,‡, Sidney H. Wang3,‡, Amy Mitrano3, Michael J. Ford4, Jonathan K. Pritchard1,2,5,§, Yoav Gilad3,§ + Author Affiliations 1Department of Genetics, Stanford University, Stanford, CA 94305, USA. 2Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA. 3Department of Human Genetics, University of Chicago, Chicago, IL 60637, USA. 4MS Bioworks, LLC, 3950 Varsity Drive, Ann Arbor, MI 48108, USA. 5Department of Biology, Stanford University, Stanford, CA 94305, USA. + Author Notes ?* Present address: Department of Computer Science, Johns Hopkins University, Baltimore, MD 21218, USA. ?† Present address: Department of Computer Science, University of Maryland, College Park, MD 20742, USA. ?§Corresponding author. E-mail: pritch@stanford.edu (J.K.P); gilad@uchicago.edu (Y.G.) ?‡ These authors contributed equally to this work. The phenotypic consequences of expression quantitative trait loci (eQTLs) are presumably due to their effects on protein expression levels. Yet, the impact of genetic variation, including eQTLs, on protein levels remains poorly understood. To address this, we mapped genetic variants that are associated with eQTLs, ribosome occupancy (rQTLs), or protein abundance (pQTLs). We found that most QTLs are associated with transcript expression levels, with consequent effects on ribosome and protein levels. However, eQTLs tend to have significantly reduced effect sizes on protein levels, suggesting that their potential impact on downstream phenotypes is often attenuated or buffered. Additionally, we identified a class of cis QTLs that affect protein abundance with little or no effect on mRNA or ribosome levels, suggesting that they may arise from differences in post-translational regulation. Received for publication 3 September 2014. Accepted for publication 9 December 2014. Published Online December 18 2014
Would anyone like to discuss thoroughly what this paper may indicate? Yes, no, maybe? :)Dionisio_{December 21, 2014
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WD400, you forget the other whopper in the OP: These results do not suggest that there is an unidentified mechanism of gene regulation. Translational regulation and protein stability has been described and studied for over 25 years. Of course if you rely on science aggregators like Phys.org that are further mangled by 'News' to get your science info... well then you get people like BA77, I guess.hrun0815_{December 19, 2014
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"The findings point to a yet-unidentified cellular mechanism that regulates gene expression and suggest studies that rely only on RNA measurements to characterize gene function require further analysis." So finding ANOTHER level of gene regulation complexity on top of what was thought to be 'only RNA' regulating gene expression is evidence for Darwinism because??,, Because?? Well because Darwinism likes extra unexpected, and overlapping, levels of complexity being discovered in cells all the time! :) Regardless of how wd400 may try to spin this, this is NOT good news for Darwinism,,, as a commenter on FB put it: 'So basically in our lifetime we've seen cells go from figurative "blocks", to Multidimensional "tools", to "flip-phones" and now its about to go to an even HIGHER state of complexity...like an "ipod".'bornagain77_{December 19, 2014
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UD is really on a roll this week... These differences are unrelated to the RNA world, but they are often cited as evidence that most of the genome is functional. "Not only is most of the genome transcribed, but there are tissue-specific differences in RNA abundance between transcripts". This paper is about between-individual differences in gene expression, but still seems to undercut this argument (which wasn't very good so start with, FWIW).wd400_{December 19, 2014
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