The multifaceted bacterial cysteine desulfurases: From metabolism to pathogenesis

Das, M and Dewan, A and Shee, S and Singh, A (2021) The multifaceted bacterial cysteine desulfurases: From metabolism to pathogenesis. In: Antioxidants, 10 (7).

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Abstract

Living cells have developed a relay system to efficiently transfer sulfur (S) from cysteine to various thio-cofactors (iron-sulfur (Fe-S) clusters, thiamine, molybdopterin, lipoic acid, and biotin) and thiolated tRNA. The presence of such a transit route involves multiple protein components that allow the flux of S to be precisely regulated as a function of environmental cues to avoid the unnecessary accumulation of toxic concentrations of soluble sulfide (S2� ). The first enzyme in this relay system is cysteine desulfurase (CSD). CSD catalyzes the release of sulfane S from L-cysteine by converting it to L-alanine by forming an enzyme-linked persulfide intermediate on its conserved cysteine residue. The persulfide S is then transferred to diverse acceptor proteins for its incorporation into the thio-cofactors. The thio-cofactor binding-proteins participate in essential and diverse cellular processes, including DNA repair, respiration, intermediary metabolism, gene regulation, and redox sensing. Additionally, CSD modulates pathogenesis, antibiotic susceptibility, metabolism, and survival of several pathogenic microbes within their hosts. In this review, we aim to comprehensively illustrate the impact of CSD on bacterial core metabolic processes and its requirement to combat redox stresses and antibiotics. Targeting CSD in human pathogens can be a potential therapy for better treatment outcomes. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Item Type:	Journal Article
Publication:	Antioxidants
Publisher:	MDPI AG
Additional Information:	The copyright for this article belongs to MDPI AG
Department/Centre:	Division of Biological Sciences > Centre for Infectious Disease Research
Date Deposited:	02 Aug 2021 11:57
Last Modified:	02 Aug 2021 11:57
URI:	http://eprints.iisc.ac.in/id/eprint/69001

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