LATEST HIGHLIGHTS

CURRENT ISSUE

The tip of the pseudopilus
Article by Korotkov and Hol

The 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.


CURRENT ISSUE

ATP-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

While 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.


CURRENT ISSUE

Cap-binding by influenza
Article by Cusack and colleagues

Influenza 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

Article by Bar-Sagi, Groves, Kuriyan and colleagues
*FREE ACCESS*

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

Nuclear 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.


CURRENT ISSUE

The signal recognition particle (SRP) is involved in membrane targeting of translating ribosomes. Peptides within the ribosome exit tunnel are shown to elicit SRP recruitment to, and membrane targeting of, translating
E. coli ribosomes independent of specific sequences in a purified system, suggesting that peptide presence within the ribosome can be conveyed externally.


INFORMATION FOR AUTHORS

Authors are encouraged to submit their version of accepted unedited NPG journal papers to PubMedCentral or other appropriate archives, for public release six months after publication. The reference, DOI number, and link to the URL on the journal's website should be provided.


This complies with NIH Public Access Policy, HHMI policy, as well as the position of the Wellcome Trust. As a service to our authors, NSMB can help upload your accepted manuscripts to PubMed Central. Please contact us at nsmb@natureny.com for further information.




Extra navigation


naturejobs

natureproducts


Advertisement

Supported by

TaqMan Gene Expression and SNP Genotyping assays are available for genes referenced in this article. Click a link below for detailed information.

Taqman Products

ADVERTISEMENT