《Nature》目录要览：2010-12-16出版
时间：2010-12-16 阅读： 我要评论:
Melanomas acquire resistance to B-RAF(V600E) inhibition by RTK or N- RAS upregulation pp973 - 977
Recent data from early clinical trials in melanoma patients carrying mutations in the B-RAF gene have shown promising results with the B- RAF kinase inhibitor PLX4032; however, many patients eventually develop resistance to this treatment. Two papers now uncover possible mechanisms of resistance to PLX4032. One paper shows that upregulation of MAP3K8 (which encodes COT) can confer resistance of melanoma cells to B-RAF inhibitors, whereas another paper found that melanomas can acquire resistance due to mutations of N-RAS or increased expression of PDGFRβ. Each of these resistance mechanisms seems to apply to at least some patients on recent PLX4032 trial, whereas, surprisingly, so far no secondary B-RAF mutations have been observed.
Ramin Nazarian et al.
doi:10.1038/nature09626
Abstract: http://www.nature.com/nature/journal/v468/n7326/abs/nature09626.html
Article: http://www.nature.com/nature/journal/v468/n7326/full/nature09626.html
Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein pp978 - 982
A crystal structure of bacterial RNA polymerase (RNAP) bound to the transcription inhibitor Gfh1 reveals the mechanism of inhibition by Gfh1 and an alternative ratcheted state of RNAP.
Shunsuke Tagami et al.
doi:10.1038/nature09573
Abstract: http://www.nature.com/nature/journal/v468/n7326/abs/nature09573.html
Article: http://www.nature.com/nature/journal/v468/n7326/full/nature09573.html
Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase pp983 - 987
Protein machineries that move along the DNA, such as DNA polymerases and helicases, will necessarily encounter other bound proteins interacting with specific sites. Using 'curtains' of labelled DNA, this study measured whether such bound proteins interfere with the activity of the bacterial DNA translocase RecBCD. The translocase is able to push the proteins over nonspecific sites for thousands of base pairs before they are displaced.
Ilya J. Finkelstein, Mari-Liis Visnapuu and Eric C. Greene
doi:10.1038/nature09561
Abstract: http://www.nature.com/nature/journal/v468/n7326/abs/nature09561.html
Article: http://www.nature.com/nature/journal/v468/n7326/full/nature09561.html
The mechanism of sodium and substrate release from the binding pocket of vSGLT pp988 - 991
Here, a comprehensive study of the sodium/galactose transporter (vSGLT) is presented, consisting of molecular dynamics simulations, biochemical characterization and a new crystal structure of the 'inward-open' conformation. These experiments show that sodium exit causes a reorientation of transmembrane helix 1, opening an inner gate required for substrate exit, while also triggering minor rigid-body movements in two sets of transmembrane helical bundles. This cascade of conformational changes is responsible for the proper timing of ion and substrate release.
Akira Watanabe et al.
doi:10.1038/nature09580
Abstract: http://www.nature.com/nature/journal/v468/n7326/abs/nature09580.html
Article: http://www.nature.com/nature/journal/v468/n7326/full/nature09580.html
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FUTURES
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Silence p996
Turn on, tune out.
John Frizell
doi:10.1038/468996a
http://www.nature.com/nature/journal/v468/n7326/full/468996a.html
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