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:
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#1 addendum
More on this:
http://www.upi.com/Science_New.....420205267/
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/cont.....0c68795868
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”).
[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/cont.....0c68795868
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”).
“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_New.....z3Nh9NFp8s
In case someone here is interested:
The Next Generation of Pathway Analysis for Integrated Omics Data
http://www.genengnews.com/webi.....-data/241/