Structural coordination of polymerization and crosslinking by a SEDS–bPBP peptidoglycan synthase complex-Reference-Cited by-同舟云学术

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Structural coordination of polymerization and crosslinking by a SEDS–bPBP peptidoglycan synthase complex

Published:2020-03-09 Issue:6 Volume:5 Page:813-820
ISSN:2058-5276
Container-title:Nature Microbiology
language:en
Short-container-title:Nat Microbiol

Author:

Sjodt Megan,Rohs Patricia D. A.,Gilman Morgan S. A.,Erlandson Sarah C.,Zheng Sanduo,Green Anna G.,Brock Kelly P.^ORCID,Taguchi Atsushi^ORCID,Kahne Daniel,Walker Suzanne^ORCID,Marks Debora S.,Rudner David Z.,Bernhardt Thomas G.^ORCID,Kruse Andrew C.^ORCID

Funder

U.S. Department of Health & Human Services | National Institutes of Health

Howard Hughes Medical Institute

Gouvernement du Canada | Canadian Institutes of Health Research

Harvard Medical School

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology

Link

http://www.nature.com/articles/s41564-020-0687-z.pdf

Reference38 articles.

1. Meeske, A. J. et al. SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature 537, 634–638 (2016).

2. Emami, K. et al. RodA as the missing glycosyltransferase in Bacillus subtilis and antibiotic discovery for the peptidoglycan polymerase pathway. Nat. Microbiol. 2, 16253 (2017).

3. Cho, H. et al. Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously. Nat. Microbiol. 1, 16172 (2016).

4. Rohs, P. D. A. et al. A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery. PLoS Genet. 14, e1007726 (2018).

5. Taguchi, A. et al. FtsW is a peptidoglycan polymerase that is functional only in complex with its cognate penicillin-binding protein. Nat. Microbiol. 4, 587–594 (2019).

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