Cargando…

Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces

The acylation of sugars, most commonly via acetylation, is a widely used mechanism in bacteria that uses a simple chemical modification to confer useful traits. For structures like lipopolysaccharide, capsule and peptidoglycan, that function outside of the cytoplasm, their acylation during export or...

Descripción completa

Detalles Bibliográficos
Autores principales: Pearson, Caroline, Tindall, Sarah, Potts, Jennifer R., Thomas, Gavin H., van der Woude, Marjan W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Microbiology Society 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9558356/
https://www.ncbi.nlm.nih.gov/pubmed/35253642
http://dx.doi.org/10.1099/mic.0.001146
_version_ 1784807426186280960
author Pearson, Caroline
Tindall, Sarah
Potts, Jennifer R.
Thomas, Gavin H.
van der Woude, Marjan W.
author_facet Pearson, Caroline
Tindall, Sarah
Potts, Jennifer R.
Thomas, Gavin H.
van der Woude, Marjan W.
author_sort Pearson, Caroline
collection PubMed
description The acylation of sugars, most commonly via acetylation, is a widely used mechanism in bacteria that uses a simple chemical modification to confer useful traits. For structures like lipopolysaccharide, capsule and peptidoglycan, that function outside of the cytoplasm, their acylation during export or post-synthesis requires transport of an activated acyl group across the membrane. In bacteria this function is most commonly linked to a family of integral membrane proteins – acyltransferase-3 (AT3). Numerous studies examining production of diverse extracytoplasmic sugar-containing structures have identified roles for these proteins in O-acylation. Many of the phenotypes conferred by the action of AT3 proteins influence host colonisation and environmental survival, as well as controlling the properties of biotechnologically important polysaccharides and the modification of antibiotics and antitumour drugs by Actinobacteria. Herein we present the first systematic review, to our knowledge, of the functions of bacterial AT3 proteins, revealing an important protein family involved in a plethora of systems of importance to bacterial function that is still relatively poorly understood at the mechanistic level. By defining and comparing this set of functions we draw out common themes in the structure and mechanism of this fascinating family of membrane-bound enzymes, which, due to their role in host colonisation in many pathogens, could offer novel targets for the development of antimicrobials.
format Online
Article
Text
id pubmed-9558356
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Microbiology Society
record_format MEDLINE/PubMed
spelling pubmed-95583562022-10-14 Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces Pearson, Caroline Tindall, Sarah Potts, Jennifer R. Thomas, Gavin H. van der Woude, Marjan W. Microbiology (Reading) Reviews The acylation of sugars, most commonly via acetylation, is a widely used mechanism in bacteria that uses a simple chemical modification to confer useful traits. For structures like lipopolysaccharide, capsule and peptidoglycan, that function outside of the cytoplasm, their acylation during export or post-synthesis requires transport of an activated acyl group across the membrane. In bacteria this function is most commonly linked to a family of integral membrane proteins – acyltransferase-3 (AT3). Numerous studies examining production of diverse extracytoplasmic sugar-containing structures have identified roles for these proteins in O-acylation. Many of the phenotypes conferred by the action of AT3 proteins influence host colonisation and environmental survival, as well as controlling the properties of biotechnologically important polysaccharides and the modification of antibiotics and antitumour drugs by Actinobacteria. Herein we present the first systematic review, to our knowledge, of the functions of bacterial AT3 proteins, revealing an important protein family involved in a plethora of systems of importance to bacterial function that is still relatively poorly understood at the mechanistic level. By defining and comparing this set of functions we draw out common themes in the structure and mechanism of this fascinating family of membrane-bound enzymes, which, due to their role in host colonisation in many pathogens, could offer novel targets for the development of antimicrobials. Microbiology Society 2022-03-07 /pmc/articles/PMC9558356/ /pubmed/35253642 http://dx.doi.org/10.1099/mic.0.001146 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution.
spellingShingle Reviews
Pearson, Caroline
Tindall, Sarah
Potts, Jennifer R.
Thomas, Gavin H.
van der Woude, Marjan W.
Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title_full Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title_fullStr Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title_full_unstemmed Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title_short Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
title_sort diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9558356/
https://www.ncbi.nlm.nih.gov/pubmed/35253642
http://dx.doi.org/10.1099/mic.0.001146
work_keys_str_mv AT pearsoncaroline diversefunctionsforacyltransferase3proteinsinthemodificationofbacterialcellsurfaces
AT tindallsarah diversefunctionsforacyltransferase3proteinsinthemodificationofbacterialcellsurfaces
AT pottsjenniferr diversefunctionsforacyltransferase3proteinsinthemodificationofbacterialcellsurfaces
AT thomasgavinh diversefunctionsforacyltransferase3proteinsinthemodificationofbacterialcellsurfaces
AT vanderwoudemarjanw diversefunctionsforacyltransferase3proteinsinthemodificationofbacterialcellsurfaces