RRC ID 35510
Author Pazos M, Natale P, Vicente M.
Title A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein.
Journal J Biol Chem
Abstract In Escherichia coli, the cell division protein FtsZ is anchored to the cytoplasmic membrane by the action of the bitopic membrane protein ZipA and the cytoplasmic protein FtsA. Although the presence of both ZipA and FtsA is strictly indispensable for cell division, an FtsA gain-of-function mutant FtsA* (R286W) can bypass the ZipA requirement for cell division. This observation casts doubts on the role of ZipA and its need for cell division. Maxicells are nucleoid-free bacterial cells used as a whole cell in vitro system to probe protein-protein interactions without the need of protein purification. We show that ZipA protects FtsZ from the ClpXP-directed degradation observed in E. coli maxicells and that ZipA-stabilized FtsZ forms membrane-attached spiral-like structures in the bacterial cytoplasm. The overproduction of the FtsZ-binding ZipA domain is sufficient to protect FtsZ from degradation, whereas other C-terminal ZipA partial deletions lacking it are not. Individual overproduction of the proto-ring component FtsA or its gain-of-function mutant FtsA* does not result in FtsZ protection. Overproduction of FtsA or FtsA* together with ZipA does not interfere with the FtsZ protection. Moreover, neither FtsA nor FtsA* protects FtsZ when overproduced together with ZipA mutants lacking the FZB domain. We propose that ZipA protects FtsZ from degradation by ClpP by making the FtsZ site of interaction unavailable to the ClpX moiety of the ClpXP protease. This role cannot be replaced by either FtsA or FtsA*, suggesting a unique function for ZipA in proto-ring stability.
Volume 288(5)
Pages 3219-26
Published 2013-2-1
DOI 10.1074/jbc.M112.434944
PII M112.434944
PMID 23233671
PMC PMC3561543
MeSH Bacterial Proteins / chemistry Bacterial Proteins / metabolism* Carrier Proteins / chemistry Carrier Proteins / metabolism* Cell Cycle Proteins / chemistry Cell Cycle Proteins / metabolism* Cell Division* Cytoskeletal Proteins / chemistry Cytoskeletal Proteins / metabolism* Escherichia coli / cytology* Escherichia coli / metabolism* Escherichia coli Proteins / chemistry Escherichia coli Proteins / metabolism* Models, Molecular Mutant Proteins / chemistry Mutant Proteins / metabolism Protein Binding Protein Stability Protein Structure, Secondary Protein Structure, Tertiary Proteolysis
IF 4.106
Times Cited 36
Prokaryotes E. coli pBAD24 pBAD33 JW0427-KC JW0428-KC