title: Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
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.
authors.affiliation: Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City 66160, USA.
authors.forename: X
authors.initials: X
authors.lastname: Wang
authors.forename: J
authors.initials: J
authors.lastname: Huang
authors.forename: A
authors.initials: A
authors.lastname: Mukherjee
authors.forename: C
authors.initials: C
authors.lastname: Cao
authors.forename: J
authors.initials: J
authors.lastname: Lutkenhaus
mesh_terms: D001216:Asparagine / Q000502:physiology; D001224:Aspartic Acid / Q000502:physiology; D001412:Bacillus subtilis; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D020558:GTP Phosphohydrolases / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000378:metabolism; D011108:Polymers; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017421:Sequence Analysis; D014357:Trypsin
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C065103:FtsA protein, Bacteria; C489310:FtsA protein, E coli; C071525:FtsZ protein, Bacteria; D010446:Peptide Fragments; D011108:Polymers; D011993:Recombinant Fusion Proteins; D001224:Aspartic Acid; D001216:Asparagine; D006160:Guanosine Triphosphate; D014357:Trypsin; D020558:GTP Phosphohydrolases