YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site.
YgbQ is a cell division protein in Escherichia coli and Vibrio cholerae. In E. coli the ygbQ gene was discovered as a result of a computer search of the E. coli genome designed to find potential interacting partners for cell division protein FtsL. In V. cholerae, ygbQ was identified as an essential gene by using a transposon that fuses genes to an arabinose promoter. The role of YgbQ in cell division is supported by the following. Cells depleted of YgbQ in both organisms form long filaments, but DNA segregation is not affected. YgbQ localizes to the constriction site in wild-type E. coli cells. Localization of E. coli YgbQ to the constriction site depends on cell division proteins FtsQ and FtsL but not FtsW and FtsI, placing YgbQ in the sequential dependency order of proteins localizing to the division site. Localization of green fluorescent protein-FtsL also depends on YgbQ, indicating that FtsL and YgbQ colocalize to the division site in E. coli. Our results show colocalization of proteins to the bacterial midcell in E. coli and raise the possibility that these proteins interact in a coiled-coil structure.
Buddelmeijer
Nienke
N
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Judson
Nicholas
N
Boyd
Dana
D
Mekalanos
John J
JJ
Beckwith
Jonathan
J
D000595:Amino Acid Sequence; D001089:Arabinose / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism*; D015153:Blotting, Western; D002352:Carrier Proteins; D018797:Cell Cycle Proteins / Q000096:biosynthesis* / Q000737:chemistry; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D019992:Databases as Topic; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000096:biosynthesis* / Q000737:chemistry; D049452:Green Fluorescent Proteins; D006602:Hexosyltransferases / Q000378:metabolism; D008164:Luminescent Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism; D002267:Muramoylpentapeptide Carboxypeptidase; D016366:Open Reading Frames; D009876:Operon; D046915:Penicillin-Binding Proteins; D046928:Peptidoglycan Glycosyltransferase; D010458:Peptidyl Transferases / Q000378:metabolism; D010641:Phenotype; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014734:Vibrio cholerae / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C456028:FtsB protein, E coli; C478704:FtsI protein, E coli; D008164:Luminescent Proteins; D008565:Membrane Proteins; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; D011993:Recombinant Fusion Proteins; C078387:ftsL protein, E coli; C061684:FtsW protein, Bacteria; D049452:Green Fluorescent Proteins; D004247:DNA; D001089:Arabinose; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D046928:Peptidoglycan Glycosyltransferase; D002267:Muramoylpentapeptide Carboxypeptidase