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Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria

Microbial biodiversity includes biotic and abiotic components that support all life forms by adapting to environmental conditions. Climate change, pollution, human activity, and natural calamities affect microbial biodiversity. Microbes have diverse growth conditions, physiology, and metabolism. Bac...

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Autores principales: Kumar, Lokender, Patel, Sanjay Kumar Singh, Kharga, Kusum, Kumar, Rajnish, Kumar, Pradeep, Pandohee, Jessica, Kulshresha, Sourabh, Harjai, Kusum, Chhibber, Sanjay
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9654057/
https://www.ncbi.nlm.nih.gov/pubmed/36364411
http://dx.doi.org/10.3390/molecules27217584
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author Kumar, Lokender
Patel, Sanjay Kumar Singh
Kharga, Kusum
Kumar, Rajnish
Kumar, Pradeep
Pandohee, Jessica
Kulshresha, Sourabh
Harjai, Kusum
Chhibber, Sanjay
author_facet Kumar, Lokender
Patel, Sanjay Kumar Singh
Kharga, Kusum
Kumar, Rajnish
Kumar, Pradeep
Pandohee, Jessica
Kulshresha, Sourabh
Harjai, Kusum
Chhibber, Sanjay
author_sort Kumar, Lokender
collection PubMed
description Microbial biodiversity includes biotic and abiotic components that support all life forms by adapting to environmental conditions. Climate change, pollution, human activity, and natural calamities affect microbial biodiversity. Microbes have diverse growth conditions, physiology, and metabolism. Bacteria use signaling systems such as quorum sensing (QS) to regulate cellular interactions via small chemical signaling molecules which also help with adaptation under undesirable survival conditions. Proteobacteria use acyl-homoserine lactone (AHL) molecules as autoinducers to sense population density and modulate gene expression. The LuxI-type enzymes synthesize AHL molecules, while the LuxR-type proteins (AHL transcriptional regulators) bind to AHLs to regulate QS-dependent gene expression. Diverse AHLs have been identified, and the diversity extends to AHL synthases and AHL receptors. This review comprehensively explains the molecular diversity of AHL signaling components of Pseudomonas aeruginosa, Chromobacterium violaceum, Agrobacterium tumefaciens, and Escherichia coli. The regulatory mechanism of AHL signaling is also highlighted in this review, which adds to the current understanding of AHL signaling in Gram-negative bacteria. We summarize molecular diversity among well-studied QS systems and recent advances in the role of QS proteins in bacterial cellular signaling pathways. This review describes AHL-dependent QS details in bacteria that can be employed to understand their features, improve environmental adaptation, and develop broad biomolecule-based biotechnological applications.
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spelling pubmed-96540572022-11-15 Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria Kumar, Lokender Patel, Sanjay Kumar Singh Kharga, Kusum Kumar, Rajnish Kumar, Pradeep Pandohee, Jessica Kulshresha, Sourabh Harjai, Kusum Chhibber, Sanjay Molecules Review Microbial biodiversity includes biotic and abiotic components that support all life forms by adapting to environmental conditions. Climate change, pollution, human activity, and natural calamities affect microbial biodiversity. Microbes have diverse growth conditions, physiology, and metabolism. Bacteria use signaling systems such as quorum sensing (QS) to regulate cellular interactions via small chemical signaling molecules which also help with adaptation under undesirable survival conditions. Proteobacteria use acyl-homoserine lactone (AHL) molecules as autoinducers to sense population density and modulate gene expression. The LuxI-type enzymes synthesize AHL molecules, while the LuxR-type proteins (AHL transcriptional regulators) bind to AHLs to regulate QS-dependent gene expression. Diverse AHLs have been identified, and the diversity extends to AHL synthases and AHL receptors. This review comprehensively explains the molecular diversity of AHL signaling components of Pseudomonas aeruginosa, Chromobacterium violaceum, Agrobacterium tumefaciens, and Escherichia coli. The regulatory mechanism of AHL signaling is also highlighted in this review, which adds to the current understanding of AHL signaling in Gram-negative bacteria. We summarize molecular diversity among well-studied QS systems and recent advances in the role of QS proteins in bacterial cellular signaling pathways. This review describes AHL-dependent QS details in bacteria that can be employed to understand their features, improve environmental adaptation, and develop broad biomolecule-based biotechnological applications. MDPI 2022-11-04 /pmc/articles/PMC9654057/ /pubmed/36364411 http://dx.doi.org/10.3390/molecules27217584 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kumar, Lokender
Patel, Sanjay Kumar Singh
Kharga, Kusum
Kumar, Rajnish
Kumar, Pradeep
Pandohee, Jessica
Kulshresha, Sourabh
Harjai, Kusum
Chhibber, Sanjay
Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title_full Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title_fullStr Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title_full_unstemmed Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title_short Molecular Mechanisms and Applications of N-Acyl Homoserine Lactone-Mediated Quorum Sensing in Bacteria
title_sort molecular mechanisms and applications of n-acyl homoserine lactone-mediated quorum sensing in bacteria
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9654057/
https://www.ncbi.nlm.nih.gov/pubmed/36364411
http://dx.doi.org/10.3390/molecules27217584
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