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 40 years, 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.

Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein / Campanini, Barbara; Benoni, Roberto; Bettati, Stefano; Beck, Christina M.; Hayes, Christopher S.; Mozzarelli, Andrea. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - 1854:9(2015), pp. 1184-1193. [10.1016/j.bbapap.2015.02.013]

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

CAMPANINI, Barbara;BENONI, Roberto;BETTATI, Stefano;MOZZARELLI, Andrea
2015

Abstract

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 40 years, 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.
Moonlighting O-acetylserine sulfhydrylase: New functions for an old protein / Campanini, Barbara; Benoni, Roberto; Bettati, Stefano; Beck, Christina M.; Hayes, Christopher S.; Mozzarelli, Andrea. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - 1854:9(2015), pp. 1184-1193. [10.1016/j.bbapap.2015.02.013]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/2796909
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