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Volume 11 Issue 10, October 2004

An artistic interpretation of a model of how RACK1 may function on the ribosome. The model is based on the cryo-EM structure of the RACK1â–ribosome complex reported by Sengupta et al. pp 957â–962.

Editorial

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  • Ubiquitin-like proteins, including NEDD8, regulate a wide range of cellular processes and are mobilized by parallel biochemical pathways. A recent crystal structure explains how the NEDD8-specific E1 enzyme specifically recruits its cognate E2 enzyme by binding to a flexible N-terminal extension.

    • Andrew P VanDemark
    • Christopher P Hill
    News & Views
  • A second high-affinity binding site for the I-TevI homing endonuclease has been discovered. Surprisingly, the DNA sequence recognized is the protein's own operator; at this site, the endonuclease represses its own transcription instead of cleaving the DNA and inducing intron homing.

    • Nikolai Windbichler
    • Renée Schroeder
    News & Views
  • A recent study of adenylate kinase reveals that conformational dynamics in control product release and determine the rate-limiting step in the overall catalytic reaction.

    • Mikael Akke
    News & Views
  • The implication of arginine methylation in mRNA biogenesis from transcription to mRNA export has been documented by various groups, but the precise role of methylation in this process is still unknown. A recent study demonstrates that in Saccharomyces cerevisiae methylation modulates the interaction and recruitment of components of the RNA packaging and export machinery.

    • Kiven E Lukong
    • Stéphane Richard
    News & Views
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