Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein

Biochimica Et Biophysica Acta
Barbara CampaniniAndrea Mozzarelli

Abstract

O-acetylserine sulfhydrylase A (CysK) is the pyridoxal 5'-phosphate-dependent enzyme that catalyzes the final reaction of cysteine biosynthesis in bacteria. CysK was initially identified in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This "cysteine synthase" complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Remarkably, the CysK/CysE binding interaction is conserved in most bacterial and plant systems. For the past 40years, CysK was thought to function exclusively in cysteine biosynthesis, but recent studies have revealed a repertoire of additional "moonlighting" activities for this enzyme. CysK and its paralogs influence transcription in both Gram-positive bacteria and the nematode Caenorhabditis elegans. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Intriguingly, each moonlighting activity requires a binding partner that invariably mimics the C-terminus of CysE to interact with the CysK active site. This article is part of a Special Issue entitled: Cofactor-dependent proteins: evolution, chemical diversity and bio-applications.

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Citations

Jun 14, 2015·Biochimica Et Biophysica Acta·Andrea Mozzarelli, Loredano Pollegioni
Aug 18, 2016·Proceedings of the National Academy of Sciences of the United States of America·Parker M JohnsonCelia W Goulding
Oct 13, 2018·Biotechnology and Applied Biochemistry·Wenjian MaXiaoyuan Wang
Jul 17, 2019·Proceedings of the National Academy of Sciences of the United States of America·Jacob R WaldbauerLichun Zhang
Nov 1, 2017·Emerging Topics in Life Sciences·Allison M JonesChristopher S Hayes
Nov 15, 2020·Expert Opinion on Therapeutic Patents·Giannamaria Annunziato, Gabriele Costantino

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