Molecular basis of the lipid-induced MucA-MucB dissociation in Pseudomonas aeruginosa.
Amino Acid Sequence
/ genetics
Bacterial Proteins
/ chemistry
Crystallography, X-Ray
Gene Expression Regulation, Bacterial
/ genetics
Hydrophobic and Hydrophilic Interactions
Lipids
/ chemistry
Mutation
/ genetics
Polyethylene Glycols
/ chemistry
Protein Binding
/ genetics
Protein Conformation
Pseudomonas aeruginosa
/ chemistry
Sigma Factor
/ chemistry
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
03 08 2020
03 08 2020
Historique:
received:
31
10
2019
accepted:
06
07
2020
entrez:
5
8
2020
pubmed:
5
8
2020
medline:
22
6
2021
Statut:
epublish
Résumé
MucA and MucB are critical negative modulators of sigma factor AlgU and regulate the mucoid conversion of Pseudomonas aeruginosa. Previous studies have revealed that lipid signals antagonize MucA-MucB binding. Here we report the crystal structure of MucB in complex with the periplasmic domain of MucA and polyethylene glycol (PEG), which unveiled an intermediate state preceding the MucA-MucB dissociation. Based on the biochemical experiments, the aliphatic side chain with a polar group was found to be of primary importance for inducing MucA cleavage. These results provide evidence that the hydrophobic cavity of MucB is a primary site for sensing lipid molecules and illustrates the detailed control of conformational switching within MucA-MucB in response to lipophilic effectors.
Identifiants
pubmed: 32747658
doi: 10.1038/s42003-020-01147-1
pii: 10.1038/s42003-020-01147-1
pmc: PMC7400510
doi:
Substances chimiques
AlgU protein, Pseudomonas aeruginosa
0
Bacterial Proteins
0
Lipids
0
MucA protein, Pseudomonas
0
Sigma Factor
0
algN protein, Pseudomonas aeruginosa
0
Polyethylene Glycols
3WJQ0SDW1A
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
418Références
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