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PMID: 8430073 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 3 ·1993-02-01 ·Pages 1053-7

Mukherjee A, Dai K, Lutkenhaus J

Abstract

FtsZ is an essential cell division protein in Escherichia coli that forms a ring structure at the division site under cell cycle control. The dynamic nature of the FtsZ ring suggests possible similarities to eukaryotic filament forming proteins such as tubulin. In this study we have determined that FtsZ is a GTP/GDP binding protein with GTPase activity. A short segment of FtsZ is homologous to a segment in tubulin believed to be involved in the interaction between tubulin and guanine nucleotides. A lethal ftsZ mutation, ftsZ3 (Rsa), that leads to an amino acid alteration in this homologous segment decreased GTP binding and hydrolysis, suggesting that interaction with GTP is essential for ftsZ function.

Related Genes
FtsZ
MeSH Terms
Bacterial Proteins/isolation & purification,metabolism Cell Division Cytoskeletal Proteins Escherichia coli/cytology,enzymology,metabolism GTP Phosphohydrolases/metabolism GTP-Binding Proteins/metabolism Guanine Nucleotides/metabolism Guanosine Diphosphate/metabolism Guanosine Triphosphate/metabolism Kinetics Mutagenesis
Chemicals
Bacterial Proteins Cytoskeletal Proteins FtsZ protein, Bacteria Guanine Nucleotides Guanosine Diphosphate Guanosine Triphosphate GTP Phosphohydrolases GTP-Binding Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mukherjee A
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66103.
Dai K
Lutkenhaus J
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35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.3.1053
Published
1993-02-01
Pages
1053-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC45809
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.90.3.1053 PMC Full Text View journal details
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