Unusual 1-3 peptidoglycan cross-links in Acetobacteraceae are made by L,D-transpeptidases with a catalytic domain distantly related to YkuD domains.

Autor:	Alamán-Zárate MG; Molecular Microbiology, Biochemistry to Disease, School of Biosciences, University of Sheffield, Sheffield, UK., Rady BJ; Molecular Microbiology, Biochemistry to Disease, School of Biosciences, University of Sheffield, Sheffield, UK., Evans CA; Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Sheffield, UK., Pian B; Department of Biological and Environmental Engineering, Cornell University, Ithaca, USA., Greetham D; Molecular Microbiology, Biochemistry to Disease, School of Biosciences, University of Sheffield, Sheffield, UK., Marecos-Ortiz S; Department of Biological and Environmental Engineering, Cornell University, Ithaca, USA., Dickman MJ; Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Sheffield, UK., Lidbury IDEA; Molecular Microbiology, Biochemistry to Disease, School of Biosciences, University of Sheffield, Sheffield, UK., Lovering AL; School of Biosciences, University of Birmingham, Birmingham, UK., Barstow BM; Department of Biological and Environmental Engineering, Cornell University, Ithaca, USA., Mesnage S; Molecular Microbiology, Biochemistry to Disease, School of Biosciences, University of Sheffield, Sheffield, UK. Electronic address: s.mesnage@sheffield.ac.uk.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2024 Jan; Vol. 300 (1), pp. 105494. Date of Electronic Publication: 2023 Nov 23.
DOI:	10.1016/j.jbc.2023.105494
Abstrakt:	Peptidoglycan is an essential component of the bacterial cell envelope that contains glycan chains substituted by short peptide stems. Peptide stems are polymerized by D,D-transpeptidases, which make bonds between the amino acid in position four of a donor stem and the third residue of an acceptor stem (4-3 cross-links). Some bacterial peptidoglycans also contain 3-3 cross-links that are formed by another class of enzymes called L,D-transpeptidases which contain a YkuD catalytic domain. In this work, we investigate the formation of unusual bacterial 1-3 peptidoglycan cross-links. We describe a version of the PGFinder software that can identify 1-3 cross-links and report the high-resolution peptidoglycan structure of Gluconobacter oxydans (a model organism within the Acetobacteraceae family). We reveal that G. oxydans peptidoglycan contains peptide stems made of a single alanine as well as several dipeptide stems with unusual amino acids at their C-terminus. Using a bioinformatics approach, we identified a G. oxydans mutant from a transposon library with a drastic reduction in 1-3 cross-links. Through complementation experiments in G. oxydans and recombinant protein production in a heterologous host, we identify an L,D-transpeptidase enzyme with a domain distantly related to the YkuD domain responsible for these non-canonical reactions. This work revisits the enzymatic capabilities of L,D-transpeptidases, a versatile family of enzymes that play a key role in bacterial peptidoglycan remodelling. Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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