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J. Biochem, 1989, Vol. 106, No. 2 349-354
© 1989 Japanese Biochemical Society

research-article

Two States of the Conformation of 21S Outer Arm Dynein Coupled with ATP Hydrolysis1

Kazuo Inaba2 and Hideo Mohri

Department of Biology, College of Arts and Sciences, The University of Tokyo Meguro-ku, Tokyo 153

2To whom correspondence should be addressed.

Tryptic digestion of 21S outer arm dynein from sea urchin sperm flagella in the presence of ATP (or ADP) and vanadate produced quite different polypeptides from those obtained in the absence of ATP (ADP) and/or vanadate (Inaba and Mohri (1989) J. Biol Chem 264, 8384–8388). The 21S dynein heavy chains were consistently digested into 165- and 135-kDa polypeptides in the absence of both ATP (ADP) and vanadate. In the presence of 2 mM ADP and 100 µM vanadate, 300-kDa polypeptide, which appeared to be a precursor of 165- and 135-kDa polypeptides, became less accessible to trypsin, and 165* and 135-kDa polypeptides were digested into 150-/148-kDa and 96-kDa polypeptides, respectively. Quantitative analysis of the degradation of 165- and 135-kDa polypeptides showed that the conformations of these polypeptides change remarkably in the presence of ATP (ADP) and vanadate, and slightly in the presence of ATP{gamma}S. Photoaffinity labeling with 8-azidoadeno-sine 5'-triphosphate and vanadate-mediated photocleavage of dynein heavy chains revealed that both adenine- and {gamma}-P, -binding sites were located on 165- and 150-/148-kDa polypeptides, but not on 135-kDa polypeptide. These results suggest that the confor-mational change occurring in the 165-kDa region on binding ATP spreads to the 135-kDa region and causes the conformational change of the 135-kDa region.

1This work was supported by Grants-in- Aid from the Ministry of Education, Science and Culture of Japan.


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