Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration.
glycolipids
membrane protein integration
protein-glycan interaction
structure-activity relationships
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
26 May 2023
26 May 2023
Historique:
received:
10
02
2023
medline:
29
5
2023
pubmed:
11
3
2023
entrez:
10
3
2023
Statut:
ppublish
Résumé
MPIase is a glycolipid involved in membrane protein integration in the inner membrane of Escherichia coli. To overcome the trace amounts and heterogeneity of natural MPIase, we systematically synthesized MPIase analogs. Structure-activity relationship studies revealed the contribution of distinctive functional groups and the effect of the MPIase glycan length on membrane protein integration activity. In addition, both the synergistic effects of these analogs with the membrane chaperone/insertase YidC, and the chaperone-like activity of the phosphorylated glycan were observed. These results verified the translocon-independent membrane integration mechanism in the inner membrane of E. coli, in which MPIase captures the highly hydrophobic nascent proteins via its characteristic functional groups, prevents protein aggregation, attracts the proteins to the membrane surface, and delivers them to YidC in order to regenerate its own integration activity.
Identifiants
pubmed: 36896742
doi: 10.1002/chem.202300437
doi:
Substances chimiques
Membrane Proteins
0
Membrane Transport Proteins
0
glycolipid MPIase
0
Escherichia coli Proteins
0
Glycolipids
0
YIDC protein, E coli
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202300437Subventions
Organisme : Japan Society for the Promotion of Science
ID : JP20K05738
Organisme : Japan Society for the Promotion of Science
ID : JP18K06143 and JP22K05323
Organisme : Japan Society for the Promotion of Science
ID : JP21H03365, JP22K19262, JP22H05392, JP22H02586 and JP22H02567
Organisme : Japan Society for the Promotion of Science
ID : JP18H04433, JP19H02843 and JP22H02213
Informations de copyright
© 2023 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.
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