Tubulin and FtsZ form a distinct family of GTPases

  title={Tubulin and FtsZ form a distinct family of GTPases},
  author={Eva Nogales and Kenneth H. Downing and Linda A Amos and Jan L{\"o}we},
  journal={Nature Structural Biology},
Tubulin and FtsZ share a common fold of two domains connected by a central helix. Structure-based sequence alignment shows that common residues localize in the nucleotide-binding site and a region that interacts with the nucleotide of the next tubulin subunit in the protofilament, suggesting that tubulin and FtsZ use similar contacts to form filaments. Surfaces that would make lateral interactions between protofilaments or interact with motor proteins are, however, different. The highly… 

Structural insights into FtsZ protofilament formation

The prokaryotic tubulin homolog FtsZ polymerizes into a ring structure essential for bacterial cell division, and the nucleotide is exchangeable, explaining why, in this filament, nucleotide hydrolysis is the rate-limiting step during FTSZ polymerization.

Polymerization of FtsZ, a Bacterial Homolog of Tubulin

This work has developed a model for the isodesmic polymerization that includes GTP hydrolysis in the scheme and predicts that unlike microtubules, FtsZ protofilaments consist of GTP-bound FTSZ subunits that hydrolyze their nucleotide only slowly and are connected by high affinity longitudinal bonds with a nanomolarK D .

Tubulin and FtsZ Superfamily of Protein Assembly Machines

Tubulin superfamily proteins share a common fold within two domains that is different from other GTPases, and assemble into microtubules and other different types of dynamic cytoskeletal filaments.

Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer.

It is shown that some of their properties are different from tubulin, such as weak dimerization and chaperone-independent folding, however, their structure is strikingly similar to tubulin including surface loops, and BtubA/B form tubulin-like protofilaments.

Lessons from bacterial homolog of tubulin, FtsZ for microtubule dynamics.

The structural and functional aspects that led to the establishment of the homology between the two proteins are explained to emphasize the network of FtsZ and microtubule studies and how they are connected.

The stathmin-derived I19L peptide interacts with FtsZ and alters its bundling.

It is demonstrated here that I19L, the most efficient of these peptides, also alters FtsZ bundling assembly in vitro, and the fine analysis of the structural differences of the complexes of I 19L with Ftsz and tubulin should help for the rational development of new specific antibiotic agents.



Atomic structures of tubulin and FtsZ.

Guanine nucleotide-dependent assembly of FtsZ into filaments

Examination of FtsZ incubated in vitro by electron microscopy revealed a guanine nucleotide-dependent assembly into protein filaments, supporting the hypothesis that the FTSZ ring is formed through self-assembly.

Protofilaments and rings, two conformations of the tubulin family conserved from bacterial FtsZ to alpha/beta and gamma tubulin

It is proposed here that both protofilaments and rings are formed by all members of the tubulin family, and that they are structurally homologous across the family.

Structure of the αβ tubulin dimer by electron crystallography

An atomic model of the αβ tubulin dimer fitted to a 3.7-Å density map obtained by electron crystallography of zinc-induced tubulin sheets is presented.

Prokaryotic homolog of tubulin? Consideration of FtsZ and glyceraldehyde 3-phosphate dehydrogenase as probable candidates.

It is reported that incubation of the GAPDH in microtubule assembly buffer causes its polymerization into filamentous structures and this indicates that similar to the FtsZ proteins, GAPDh also exhibits a number of intriguing similarities to the tubulins.

Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.

The similarity of polymers formed by FtsZ and tubulin implies that the protofilament sheet is an ancient cytoskeletal system, originally functioning in bacterial cell division and later modified to make microtubules.

Structure of tubulin at 6.5 Å and location of the taxol-binding site

A three-dimensional reconstruction of tubulin to 6.5 Å resolution is presented, obtained by electron crystallography of zinc-induced two-dimensional crystals of the protein.