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Welcome to EMBO reports
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Protein Modifications: Beyond the Usual Suspects
We are pleased to announce the first EMBO Reports web focus on the topic of protein modifications. Authored by leading researchers, the series of comprehensive and engaging reviews highlights the immense complexity of post-translational protein modifications and acquaints readers with the nature and function of lesser known ones. To view and access the full list of articles and related NPG content please visit the new web focus section!
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Water, the invisible problem
Do-it-yourself biology 
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Science and Society in full... |
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Nuclear pores impact development and disease
Linear ubiquitination & NF-κB activation
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Reviews in full... |
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MAPL is a mitochondrial SUMO E3 ligase
The regulation of mitochondrial shape and function is known to involve a number of post-translational modifications, including SUMOylation. Work from the McBride lab has now characterized the first mitochondrial-anchored SUMO E3 ligase, which modifies a number of substrates including the fission GTPase DRP1 that promotes mitochondrial fragmentation.
Also in this issue: Liu & Scorrano analyse the significance of these findings.
The SecY complex selectively conducts small anions
Dalal & Duong report that the SecY translocon, which transports proteins across the bacterial inner membrane, also forms an ion channel with specificity for chloride and other small monovalent anions. Ion-specific conductance occurs at the onset of protein translocation and also across the archaeal SecY complex, and seems to be a normal consequence of protein translocation. The ionic selectivity may explain why cells tolerate mutant channels synthesized with imperfect seals.
HP1α–CAF1–SetDB1 complex provides H3K9me1
Work from the Almouzni group identifies a complex containing HP1α, CAF–1 and SetDB1 (an H3K9 methyltransferase) that monomethylates free histone H3K9, which is subsequently trimethylated by the histone methyltransferase Suv39H1. These data support a model in which the establishment and maintenance of H3K9me3 in pericentric heterochromatin occurs in a stepwise manner. The presence of CAF–1, HP1α, and SetDB1 in one complex suggests a highly co-ordinated mechanism for the propagation of H3K9me3 during DNA replication.
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| Scientific Reports in full... |
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 Science and Society Special Issue
Volume 9, July 2008
The future of our species
Click here to view Special Issue
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The EMBO Journal is a print and online publication dedicated to providing a variety of complete and rapidly published articles in all areas of molecular biology. It is one of the most highly cited journals, reflected in its latest impact factor of 8.295*
*2008 Journal Citation Reports (Thomson Reuters 2009)
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