Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin.

Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Research Abstract Details 

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Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Abstract Text:

Y Fukui,F 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 KCl 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 alpha-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 Ser1 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. 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.

Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Publishing Authors By Initials

Y Fukui,F Morita,

For similar animals: chordata: vertebrates: mammals: artiodactyla: swine research abstracts see: animals: chordata: vertebrates: mammals: artiodactyla: swine research

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Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 119

Page Numbers: 783-90

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 1996

Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Keywords Mesh Terms:

KEYWORDS: Swine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin. Information

Substance Name: Acid Phosphatase

Registry Number: EC 3.1.3.2

Grant and Affiliation Information for Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin.

AFFILIATION: Division of Chemistry, Graduate School of Science, Hokkaido University.

Country: JAPAN

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MEDLINETA: J Biochem

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