Structure of the α-, β-, and γ-heavy chains of 22 S outer arm dynein obtained from Tetrahymena cilia

摘要: Abstract Here we document the UV-induced, vanadate-dependent cleavage of alpha-, beta-, and gamma-heavy chains 22 S outer arm dynein obtained from Tetrahymena cilia. All three polypeptides have a single site photocleavage in presence Mg2+, ATP, vanadate (termed V1 cleavage). The alpha-chain yields complementary fragments with masses 232 185 kDa, beta-chain has 225 195 gamma-chain 242 161 kDa. In absence only undergoes cleavage. one V2 cleavage, which are unaffected by nucleotide require Mn2+ vanadate. always occurs on larger is separated 52, 48, 57 kDa for chains, respectively. We also found third type UV-induced termed VMT when bound to microtubules an ATP-sensitive manner under solution conditions that should support (i.e. vanadate, ATP). Under these all occur. This first documented evidence occurring implies change structure it binds microtubule. Using combination polyclonal monoclonal antibodies, been able construct linear polypeptide maps heavy chains. Their relationship previously Chlamydomonas sea urchin axonemes discussed.