Nature Structural & Molecular Biology - CURRENT ISSUE : May 2008 - Vol 15 No 5
LATEST HIGHLIGHTS
CURRENT ISSUE
The tip of the pseudopilus
Article by Korotkov and HolThe bacterial type 2 secretion system (T2SS) exports proteins across the outer membrane. The T2SS includes the pseudopilus, a structure formed by a major pseudopilin protein and a few minor ones. The crystal structure of a complex formed by three minor pseudopilins from E. coli now indicates their localization and function in the pseudopilus.
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News and Views by ForestCURRENT ISSUE
Making fork progress
Article by Tsukiyama and colleaguesATP-dependent chromatin remodelers disrupt histone-DNA contacts and have been implicated in many nuclear processes. Genome-wide analysis of replication progression and other data now indicate that two yeast remodeling complexes, Ino80 and Isw2, work in parallel to promote replication fork progression.
CURRENT ISSUE
Getting a B Complex
Article by Lührmann and colleaguesWhile it is known that phosphorylation is key to spliceosomal assembly, the targets and mechanistic basis of this has been unclear. The SRPK2 kinase is here shown to target PRP28, thus stabilizing its association with the tri-snRNP and promoting tri-snRNP integration into the spliceosome.
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News and Views by Maeder and GuthrieCURRENT ISSUE
Cap-binding by influenza
Article by Cusack and colleaguesInfluenza virus "snatches" the 5'cap from host pre-mRNAs to prime viral transcription. A domain in viral polymerase PB2 with cap-binding activity is now identified, and its crystal structure bound to a cap analog is solved.
ARTICLE OF THE MONTH
Ras activation depends on its interaction with SOS. Data now show that when Ras is membrane-bound, the activity of the SOS catalytic unit is up to 500-fold higher than rates in solution. Further analyses indicate how membrane recruitment of SOS through Ras and PIP2 work cooperatively to control SOS activity.
CURRENT ISSUE
ARPing on
Article by Cairns and colleaguesNuclear actin related proteins (ARPs) associate with a subset of chromatin remodeling and modification complexes. Here HSA domains are found to provide a conserved platform for specifically recruiting the set of ARPs or actin peculiar to a given remodeler or modification complex.
