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PMID: 9287012 Published · ppublish English Journal Article

Analysis of the interaction of FtsZ with itself, GTP, and FtsA.

Journal of bacteriology ·Vol. 179 ·No. 17 ·1997-09-00 ·Pages 5551-9

Wang X, Huang J, Mukherjee A, Cao C, Lutkenhaus J

Abstract

The interaction of FtsZ with itself, GTP, and FtsA was examined by analyzing the sensitivity of FtsZ to proteolysis and by using the yeast two-hybrid system. The N-terminal conserved domain consisting of 320 amino acids bound GTP, and a central region of FtsZ, encompassing slightly more than half of the protein, was cross-linked to GTP. Site-directed mutagenesis revealed that none of six highly conserved aspartic acid and asparagine residues were required for GTP binding. These results indicate that the specificity determinants for GTP binding are different than those for the GTPase superfamily. The N-terminal conserved domain of FtsZ contained a site for self-interaction that is conserved between FtsZ proteins from distantly related bacterial species. FtsZ320, which was truncated at the end of the conserved domain, was a potent inhibitor of division although it expressed normal GTPase activity and could polymerize. FtsZ was also found to interact directly with FtsA, and this interaction could also be observed between these proteins from distantly related bacterial species.

MeSH Terms
Asparagine/physiology Aspartic Acid/physiology Bacillus subtilis Bacterial Proteins/chemistry,genetics,metabolism Cytoskeletal Proteins Escherichia coli Escherichia coli Proteins GTP Phosphohydrolases/metabolism Guanosine Triphosphate/metabolism Mutagenesis, Site-Directed Peptide Fragments/metabolism Polymers Protein Binding Recombinant Fusion Proteins/metabolism Sequence Analysis Trypsin
Chemicals
Bacterial Proteins Cytoskeletal Proteins Escherichia coli Proteins FtsA protein, Bacteria FtsA protein, E coli FtsZ protein, Bacteria Peptide Fragments Polymers Recombinant Fusion Proteins Aspartic Acid Asparagine Guanosine Triphosphate Trypsin GTP Phosphohydrolases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wang X
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160, USA.
Huang J
Mukherjee A
Cao C
Lutkenhaus J
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.179.17.5551-5559.1997
Published
1997-09-00
Pages
5551-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC179428
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.179.17.5551-5559.1997 PMC Full Text View journal details
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