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Metabolism, cytoskeleton and cellular signalling in the grip of protein N ϵ ‐ and O‐acetylation
Author(s) -
Yang XiangJiao,
Grégoire Serge
Publication year - 2007
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400977
Subject(s) - acetylation , histone acetyltransferases , biology , histone , biochemistry , phosphorylation , microbiology and biotechnology , kinase , lysine , amino acid , dna , gene
Acetylation of the ϵ‐amino group of lysine residues (N ϵ ‐acetylation) is a reversible post‐translational modification with the potential to rival phosphorylation. In addition to histones and many transcription factors such as p53, regulators of DNA repair, replication and recombination are subject to N ϵ ‐acetylation. This modification is also important for governing the activities of various enzymes, including histone acetyltransferases, histone deacetylases, bacterial and mammalian acetyl‐CoA synthases, kinases, phosphatases, the ubiquitin ligase murine double minute 2 and the chaperonin heat shock protein 90. Furthermore, lysine acetylation occurs in cellular structure proteins such as α‐tubulin, actin, cortactin and p120 catenin. Strikingly, the Yersinia outer protein YopJ promotes O‐acetylation of crucial serine and threonine residues that are required for activation of the MAPK/ERK kinase and IκB kinase families, which precludes their phosphorylation and blocks signal transduction. Thus, N ϵ ‐ and O‐acetylation are becoming recognized as two prominent mechanisms for regulating protein functions in diverse organisms.