caa a22 4500 397557299 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021308 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021308 Two Phosphorylations Specific to the Tail Region of the 204-kDa Heavy Chain Isoform of Porcine Aorta Smooth Muscle Myosin [Elektronische Daten] [Yasuhiro Fukui, Fumi Morita] In a porcine aorta extract, we observed two protein kinase activities which specifically phosphorylate the 204-kDa heavy chain isoform of aorta myosin in the absence of conventional kinase activators. We referred to these two protein kinases, eluted at 0.15 and 0.2 M KC1 from a DEAE-column, as myosin kinases I (MKI) and II (MKII), respectively. The phosphorylation site for MKI was determined using a purified phosphopeptide derived from porcine aorta myosin phosphorylated with MKI. By comparison with the deduced amino acid sequence for smooth muscle myosins, the site corresponded to a Ser located at 3 amino acids upstream from a Pro, the putative end of the a-helical segment of the 204-kDa heavy chain tail. A homologous Ser is only present in smooth muscle myosins, i.e. not in nonmuscle myosins. MKI was purified 130-fold, but not separated from a kinase activity phosphorylating Serl or Ser2 in the 20-kDa regulatory light chain of aorta myosin. In contrast, MKII was purified to near homogeneity. MKII phosphorylated the porcine aorta myosin heavy chain at a Ser 19 amino acids downstream from the MKI site. The amino acid sequence around the Ser shared a consensus sequence of the phosphorylation site for casein kinase II and was homologous to that reported for bovine aorta myosin [Kelley, C.A. and Adelstein, R.S. (1990) J. Biol. Chem. 265, 17876-17882]. MKII was identified as a multifunctional protein kinase, casein kinase II. © by the Journal of Biochemistry Regular Papers nationallicence aorta smooth muscle nationallicence casein kinase II nationallicence myosin heavy chain nationallicence phosphorylation nationallicence protein kinase nationallicence Fukui Yasuhiro Division of Chemistry, Graduate School of Science; Hokkaido University, Sapporo, Hokkaido 060 aut Morita Fumi Division of Chemistry, Graduate School of Science; Hokkaido University, Sapporo, Hokkaido 060 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 783-790 0021-924X 119:4<783 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021308 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021308 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Fukui Yasuhiro Division of Chemistry, Graduate School of Science; Hokkaido University, Sapporo, Hokkaido 060 aut NATIONALLICENCE 700 1- Morita Fumi Division of Chemistry, Graduate School of Science; Hokkaido University, Sapporo, Hokkaido 060 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 783-790 0021-924X 119:4<783 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford