title: ZipA is required for FtsZ-dependent preseptal peptidoglycan synthesis prior to invagination during cell division.
abstract: Rod-shaped bacteria grow by a repetitive cycle of elongation followed by division, and the mechanisms responsible for these two processes have been studied for decades. However, little is known about what happens during the transition between the two activities. At least one event occurs after elongation ends and before division commences, that being the insertion of new cell wall peptidoglycan into a narrowly circumscribed ribbon around midcell where septation is destined to take place. This insertion does not depend on the presence of the septation-specific protein PBP3 and is therefore known as PBP3-independent peptidoglycan synthesis (PIPS). Here we report that only FtsZ and ZipA are required to generate PIPS in wild-type Escherichia coli. PIPS does not require the participation of other members of the divisome, the MreB-directed cell wall elongation complex, alternate peptidoglycan synthases, the major peptidoglycan amidases, or any of the low-molecular-weight penicillin binding proteins. ZipA-directed PIPS may represent an intermediate stage that connects cell wall elongation to septal invagination and may be the reason ZipA is essential in the gammaproteobacteria.
authors: Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
authors: Lakshmi-Prasad
authors: LP
authors: Potluri
authors: Suresh
authors: S
authors: Kannan
authors: Kevin D
authors: KD
authors: Young
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000235:genetics / Q000378:metabolism; D046915:Penicillin-Binding Proteins / Q000235:genetics / Q000378:metabolism; D010457:Peptidoglycan / Q000096:biosynthesis*; D046928:Peptidoglycan Glycosyltransferase / Q000235:genetics / Q000378:metabolism; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C489310:FtsA protein, E coli; C071525:FtsZ protein, Bacteria; D046915:Penicillin-Binding Proteins; D010457:Peptidoglycan; C103795:ZipA protein, E coli; D046928:Peptidoglycan Glycosyltransferase; C575488:penicillin-binding protein 1A, E coli; C478681:penicillin-binding protein 1B, E coli; D010450:Endopeptidases; C454699:EnvC protein, E coli; D046929:Serine-Type D-Ala-D-Ala Carboxypeptidase; D009238:N-Acetylmuramoyl-L-alanine Amidase