| Literature DB >> 18208400 |
Naoki Numata1, Takahide Kon, Tomohiro Shima, Kenji Imamula, Toshifumi Mogami, Reiko Ohkura, Keiko Sutoh, Kazuo Sutoh.
Abstract
Dynein is an AAA+ (ATPase associated with various cellular activities)-type motor complex that utilizes ATP hydrolysis to actively drive microtubule sliding. The dynein heavy chain (molecular mass >500 kDa) contains six tandemly linked AAA+ modules and exhibits full motor activities. Detailed molecular dissection of this motor with unique architecture was hampered by the lack of an expression system for the recombinant heavy chain, as a result of its large size. However, the recent success of recombinant protein expression with full motor activities has provided a method for advances in structure-function studies in order to elucidate the molecular mechanism of force generation.Entities:
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Year: 2008 PMID: 18208400 DOI: 10.1042/BST0360131
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407