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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 RACK1âribosome complex reported by Sengupta et al. pp 957â962.
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.
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.
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.
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.
The human Kv1.1 potassium channel undergoes RNA editing in its pore domain. Editing replaces an isoleucine with a valine that results in rapid recovery from fast inactivation.