Uncommon Descent Serving The Intelligent Design Community

When biologists forget that the Darwin cops might be listening …

Share
Facebook
Twitter
LinkedIn
Flipboard
Print
Email

They write stuff like this,  – true but politically incorrect:

The flexibility of tubulin and the consequent versatility of its self-assembly can hardly be an accident. We propose that the polymorphism of assembly unique to tubulin reflects an exquisite tuning mechanism for the complex interaction of different microtubule intermediates with cellular factors that need to detect or make direct use of the growing or shortening state of microtubules to play functional roles at the right time and place in the cell.

A friend sent this in, in response to this vid from Shawnee State University:

Follow UD News at Twitter!

Comments
In case someone here is interested: The Next Generation of Pathway Analysis for Integrated Omics Data http://www.genengnews.com/webinars/the-next-generation-of-pathway-analysis-for-integrated-omics-data/241/Dionisio
January 2, 2015
January
01
Jan
2
02
2015
11:55 AM
11
11
55
AM
PST
"This surprising discovery reflects how incomplete our understanding of biology is," study author Peter Shen, a biochemistry researcher at the University of Utah, said in a recent press release. Read more: http://www.upi.com/Science_News/2015/01/02/Researchers-find-protein-capable-of-editing-other-proteins/7181420205267/#ixzz3Nh9NFp8sDionisio
January 2, 2015
January
01
Jan
2
02
2015
11:45 AM
11
11
45
AM
PST
[research] work uncovers an unexpected mechanism of protein synthesis, in which a protein—not an mRNA—determines tRNA recruitment Science 2 January 2015: Vol. 347 no. 6217 pp. 75-78 DOI: 10.1126/science.1259724 Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains http://www.sciencemag.org/content/347/6217/75.abstract?sid=e0929331-cb7c-4b8a-9c12-e00c68795868 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. [research] 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”).Dionisio
January 2, 2015
January
01
Jan
2
02
2015
11:13 AM
11
11
13
AM
PST
Science 2 January 2015: Vol. 347 no. 6217 pp. 75-78 DOI: 10.1126/science.1259724 Rqc2p and 60S ribosomal subunits mediate mRNA-independent elongation of nascent chains http://www.sciencemag.org/content/347/6217/75.abstract?sid=e0929331-cb7c-4b8a-9c12-e00c68795868 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”).Dionisio
January 2, 2015
January
01
Jan
2
02
2015
11:12 AM
11
11
12
AM
PST
#1 addendum More on this: http://www.upi.com/Science_News/2015/01/02/Researchers-find-protein-capable-of-editing-other-proteins/7181420205267/Dionisio
January 2, 2015
January
01
Jan
2
02
2015
11:06 AM
11
11
06
AM
PST
Biological Find Defies Textbooks Results from a study published today 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, a postdoctoral fellow in biochemistry at the Univ. of Utah. “Nature [?] is capable of more than we realize.” http://www.laboratoryequipment.com/news/2015/01/biological-find-defies-textbooks?et_cid=4345947&et_rid=653535995&type=cta
Dionisio
January 2, 2015
January
01
Jan
2
02
2015
10:59 AM
10
10
59
AM
PST

Leave a Reply