Ontology highlight
ABSTRACT:
SUBMITTER: Eckert T
PROVIDER: S-EPMC3406712 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Eckert Thomas T Link Susanne S Le Doan Tuong-Van DT Sobczak Jean-Philippe JP Gieseke Anja A Richter Klaus K Woehlke Günther G
The Journal of biological chemistry 20120527 31
Spastin is a hexameric ring AAA ATPase that severs microtubules. To see whether the ring complex funnels the energy of multiple ATP hydrolysis events to the site of mechanical action, we investigate here the cooperativity of spastin. Several lines of evidence indicate that interactions among two subunits dominate the cooperative behavior: (i) the ATPase activity shows a sigmoidal dependence on the ATP concentration; (ii) ATPγS displays a mixed-inhibition behavior for normal ATP turnover; and (ii ...[more]