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The Escherichia coli Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome.
- Source :
-
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 09; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 09. - Publication Year :
- 2021
-
Abstract
- The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In Escherichia coli , it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E). Using BAM-specific antibodies, in E. coli cells, the complex is shown to localize in the lateral wall in foci. The machinery was shown to be enriched at midcell with specific cell cycle timing. The inhibition of septation by aztreonam did not alter the BAM midcell localization substantially. Furthermore, the absence of late cell division proteins at midcell did not impact BAM timing or localization. These results imply that the BAM enrichment at the site of constriction does not require an active cell division machinery. Expression of the Tre1 toxin, which impairs the FtsZ filamentation and therefore midcell localization, resulted in the complete loss of BAM midcell enrichment. A similar effect was observed for YidC, which is involved in the membrane insertion of cell division proteins in the inner membrane. The presence of the Z-ring is needed for preseptal peptidoglycan (PG) synthesis. As BAM was shown to be embedded in the PG layer, it is possible that BAM is inserted preferentially simultaneously with de novo PG synthesis to facilitate the insertion of OMPs in the newly synthesized outer membrane.
- Subjects :
- Bacterial Outer Membrane Proteins genetics
Bacterial Proteins ultrastructure
Cell Division genetics
Cytoskeletal Proteins ultrastructure
Escherichia coli chemistry
Escherichia coli genetics
Escherichia coli Infections genetics
Escherichia coli Infections microbiology
Escherichia coli Proteins ultrastructure
Gram-Negative Bacteria genetics
Gram-Negative Bacteria ultrastructure
Lipoproteins genetics
Lipoproteins ultrastructure
Membrane Transport Proteins ultrastructure
Protein Folding
Protein Multimerization genetics
Bacterial Outer Membrane Proteins ultrastructure
Bacterial Proteins genetics
Cytoskeletal Proteins genetics
Escherichia coli Proteins genetics
Membrane Transport Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1422-0067
- Volume :
- 22
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- International journal of molecular sciences
- Publication Type :
- Academic Journal
- Accession number :
- 34829983
- Full Text :
- https://doi.org/10.3390/ijms222212101