The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation inPseudomonas aeruginosa-Reference-Cited by-同舟云学术

The bacterial septal ring protein RlpA is a lytic transglycosylase that contributes to rod shape and daughter cell separation inPseudomonas aeruginosa

Published:2014-05-23 Issue:1 Volume:93 Page:113-128
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Molecular Microbiology

Author:

Jorgenson Matthew A.¹,Chen Yan²,Yahashiri Atsushi¹,Popham David L.²,Weiss David S.¹

Affiliation:

1. Department of Microbiology; Carver College of Medicine; The University of Iowa; Iowa City IA 52242 USA

2. Department of Biological Sciences; Virginia Tech; Blacksburg VA 24061 USA

Funder

National Institutes of Health

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Reference76 articles.

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2. Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA;Arends;J Bacteriol,2010

3. High-resolution crystal structure of MltE, an outer membrane-anchored endolytic peptidoglycan lytic transglycosylase from Escherichia coli;Artola-Recolons;Biochemistry,2011

4. Cooperativity of peptidoglycan synthases active in bacterial cell elongation;Banzhaf;Mol Microbiol,2012

5. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway;Bernhardt;Mol Microbiol,2003

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