Tubulin and FtsZ form a distinct family of GTPases

By E. Nogales, K. Downing, L. Amos, J. Löwe. 1998

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Cytokinesis in Bacteria (2003, background): “The great overall structural similarity between FtsZ and tubulin is described in detail elsewhere (131).”
Human RAS Superfamily Proteins and Related GTPases (2004, background): “T. Urano, R. Emkey, L. A. Feig, Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation.”
Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain (2004, background): “Second, the relative orientation of the three tubulin subunit domain”
Prokaryotic origin of the actin cytoskeleton (2001, background): “A low degree of conservation in the protofilament interface has also been found for filaments of FtsZ and tubuli”
Bacterial cell division: assembly, maintenance and disassembly of the Z ring (2009, background): “Although the carboxy-terminal domain of FtsZ is similar in its fold and acidic nature to that of tubulin, it lacks the extended surface loops that are thought to aid the assembly of the microtubule and its interaction with motor protein”
Orthologs, Paralogs, and Evolutionary Genomics 1 (2005, background): “The drastic change of function in eukaryotes apparently had been accompanied by a burst of sequence evolution such that an unequivocal demonstration of the homology of FtsZ and tubulin became possible only through comparison of the respective protein structures (65).”