Ontology highlight
ABSTRACT:
SUBMITTER: Cho C
PROVIDER: S-EPMC2533788 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20080723 38
The heavy chain of cytoplasmic dynein contains four nucleotide-binding domains referred to as AAA1-AAA4, with the first domain (AAA1) being the main ATP hydrolytic site. Although previous studies have proposed regulatory roles for AAA3 and AAA4, the role of ATP hydrolysis at these sites remains elusive. Here, we have analyzed the single molecule motility properties of yeast cytoplasmic dynein mutants bearing mutations that prevent ATP hydrolysis at AAA3 or AAA4. Both mutants remain processive, b ...[more]