Multiple sites of phosphorylation within the alpha heavy chain of Chlamydomonas outer arm dynein.
作者： S.M. King , G.B. Witman
DOI: 10.1016/S0021-9258(17)37707-4
关键词: Alpha (ethology) 、 Phosphorylation 、 Biology 、 Trypsin 、 Molecular biology 、 Chlamydomonas 、 Dynein 、 Dynein ATPase 、 Flagellum 、 Kinase 、 Biophysics
摘要: We have examined the phosphorylation of alpha dynein heavy chain (DHC) from outer arm Chlamydomonas flagellum. Quantitative analysis indicates that this DHC is phosphorylated at a minimum six sites. Using previously identified proteolytic and photocleavage sites (King, S. M., Witman, G. B. (1988) J. Biol. Chem. 263, 9244-9255), we mapped two regions are in vivo. One located 20-kDa section immediately N-terminal to site V1 photocleavage. Thus, region close ATP hydrolytic also predicted junction between head stem domains particle. The second encompasses 90-kDa C-terminal molecule. In latter section, least one found an approximately 2-kDa adopt coiled-coil structure those DHCs been sequenced. specifically labeled by endogenous kinases demembranated, washed axonemes, suggesting kinase to, or component of, situ.
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