Ontology highlight
ABSTRACT:
SUBMITTER: Schlieper D
PROVIDER: S-EPMC1166614 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Schlieper Daniel D Oliva María A MA Andreu José M JM Löwe Jan J
Proceedings of the National Academy of Sciences of the United States of America 20050620 26
alphabeta-Tubulin heterodimers, from which the microtubules of the cytoskeleton are built, have a complex chaperone-dependent folding pathway. They are thought to be unique to eukaryotes, whereas the homologue FtsZ can be found in bacteria. The exceptions are BtubA and BtubB from Prosthecobacter, which have higher sequence homology to eukaryotic tubulin than to FtsZ. Here we show that some of their properties are different from tubulin, such as weak dimerization and chaperone-independent folding ...[more]