Molecules of Bacterial

Cell Division

  [Home]  [MRC-LMB]  [Science links]  [Search engines]

A brief summary of molecules involved in bacterial cell division.

Apologies to everyone for not providing proper references. These and more complete information can be found in recent reviews of the field:

Donachie, W.D. (1993) Annual Review of Microbiology 47, 199-230

Lutkenhaus, J. and Addinall, S.G. (1997) Annual Review of Biochemistry 66, 93-116

Bramhill, D. (1997) Annual Review of Cell and Developmental Biology 13, 395-424

Rothfield, L., Justice, S. and GarciaLara, J. (1999) Annual Review of Genetics 33, 423-448.

Schematic overview:

Also consult Harold P. Erickson's webpage on "Cell division proteins present and absent in bacterial genomes"

Bacterial cell division A-Z Molecules are listed in the order of their recruitment to the septum. Annotation refers to Escherichia coli proteins, if not stated otherwise.

MinE - cell division topological specificity factor - 88 residues, 10.2kDa, SWISSPROT: MINE_ECOLI - prevents cell division inhibitor MinCD to inhibit FtsZ polymerisation at midcell - mechanism of location unknown - membrane associated, but not transmembrane - not well conserved - 3D structure: NMR structure of the 'topological specificity domain' of MinE: PDB 1EV0

MinC - forms active cell division inhibitor MinCD with MinD - a lot of bacteria do not have MinC but MinD - 231 residues, 24.8kDa, SWISSPROT: MINC_ECOLI - interacts directly with FtsZ

MinD - 269 residues, 29.5kDa, SWISSPROT: MIND_ECOLI - forms active cell division inhibitor MinCD with MinC - highly conserved - ATP binding, P-loop - 3D structure: predicted similarity to nitrogenase iron protein (PDB 1N2C)

FtsZ - backbone of the bacterial septum - forms Z-ring inside the bacterial cell - bacterial tubulin homologue - 383 residues, 40.3kDa, SWISSPROT: FTSZ_ECOLI - 3D structure similar to tubulin - conserved motif at the C-terminus: ZipA/FtsA interaction - protofilament structure similar to tubulin protofilaments - assembles into tubes, sheets, and protofilaments GTP dependent, dynamic - GTPase - 3D structure: crystal structure of FtsZ from Methanococcus jannashii FtsZ1: PDB 1FSZ

ZipA - not conserved - intercats directly with C-terminal 10 residues of FtsZ - inhibitor of FtsZ polymerization - 328 residues, 36.4kDa, SWISSPROT: ZIPA_ECOLI - 3D structure: crystal structure of ZipA in complex with a C-terminal FtsZ peptide: PDB 1F46, 1F47 - 3D structure: NMR structure of the C-terminaal domain of ZipA: PDB 1F7W, 1F7X

FtsA - 420 residues, 45.3kDa, SWISSPROT: FTSA_ECOLI - interacts directly with FtsZ - 3D structure: similarity to actin - ATP binding, actin family of proteins - 3D structure: crystal structure of FtsA from Thermotoga maritima: PDB 1E4G, 1E4F

FtsK - 1329 residues, 146.7kDa, SWISSPROT: FTSK_ECOLI - transmembrane protein: 5-6 transmembrane segments in N-terminal half. - ATP binding motif - part of SOS stress response - role in DNA replication/recombination

FtsQ - functional homologue divIB in B. subtilis - 276 residues, 31.4 kDa, SWISSPROT: FTSQ_ECOLI - transmembrane: single membrane anchor 25-49

FtsL - 121 residues, 13.6 kDa, SWISSPROT: FTSL_ECOLI - not stable - transmembrane: single transmembrane anchor 38-57

FtsI (PBP3) - penecillin binding protein - transmembrane: single traansmembrane anchor 19-39 - 588 residues, 63.9kDa, SWISSPROT: PBP3_ECOLI - synthesis of cross linked peptidoglykan from the lipid intermediates - N-terminal: transglycosylsae, C-terminal: transpepidase - transpeptidase is penicillin sensitive

FtsN - transmembrane: single transmembrane anchor 29-55 - 319 residues, 35.8kDa, SWISSPROT: FTSN_ECOLI

FtsW - time of recruitment not exactly known, some evidence for EARLY recruitment - transmembrane: 10-11 transmembrane segments with loops <60 aa - 414 residues, kDa, SWISSPROT: FTSW_ECOLI

SMC/MukB - MukB is the SMC homologue in E. coli - MukB forms MukBEF complex, no cofactors in other bacteria so far - 1486 residues, 170.2 kDa, SWISSPROT: MUKB_ECOLI - coiled-coil: antiparallel coiled-coil segements connecting N-, hinge, and C-terminal globular domains - N-and C-terminal parts come together at both ends to form ABC ATPase fold - ATP/DNA binding - eukaryotic homologues in sister chromatid cohesion (cohesin), chromosome condensation (condensin) and double strand break repair. - ATP dependent DNA aggregation - 3D structure: crystal structure of the catalytic domain of Rad50: PDB 1F2T, 1F2U - 3D structure: crystal structure of the SMC head domain from T. maritima: PDB 1E69