Mapping phosphorylation site of the regulatory light chain in smooth muscle myosin by immuno-electron microscopy
スポンサーリンク
概要
- 論文の詳細を見る
Phosphorylation site responsible for the regulation of smooth muscle myosin was mapped using a polyclonal antibody against a phosphorylated hendecapeptide corresponding to the amino acid sequence around Ser-19 in the regulatory light chain. Phosphorylated myosin mixed with the antibody was rotary-shadowed and was examined by electron microscopy. The antibody binding site was located in the head portion of myosin and the average distance from the head-rod junction was about 3nm toward the tip of myosin head. The results indicate that the phosphorylated Ser-19 in regulatory light chain is a little more extended toward the adjacent essential light chain in reference to the resolved N-terminal residues of the regulatory light chain in the three dimensional structure of myosin heads from other sources, in which the structure of the N-terminal portions homologous to the phosphorylated Ser-19 was not resolved (Rayment, I. et al. (1993) Science 261, 50-58; Xie, X. et al. (1994) Nature 368, 306-312). Intramolecular interaction through the introduced phosphoryl group may be the primary results in the regulatory light chain which releases the motor domain from its suppressed state.
- 日本学士院の論文
著者
-
YAZAWA Michio
Division of Chemistry, Graduate School of Science, Hokkaido University
-
MORITA Fumi
Division of Chemistry, Graduate School of Science, Hokkaido University
-
Morita F
Hokkaido Univ. Hokkaido
-
Yazawa Michio
Division Of Chemistry Graduate School Of Science Hokkaido University
-
Katoh T
Department Of Biochemistry Asahikawa Medical College
-
Katoh Tsuyoshi
Division Of Chemistry Graduate School Of Science Hokkaido University
-
Tsuyoshi Katoh
Department Of Biochemistry Asahikawa Medical College
-
WATANABE Michitoshi
Division of Chemistry, Graduate School of Science, Hokkaido University
-
Morita Fumi
Division Of Chemistry Graduate School Of Sciemce Hokkaido University
-
Yazawa Michio
Division Of Chemistry Faculty Of Science Hokkaido University
関連論文
- Reactivies of Cys^ (SH1) in Intermediate States of Myosin Subfragment-1 ATPase
- Localization of 17-kDa Myosin Light Chain Isoforms in Cultured Aortic smooth Muscle Cells
- Secondary Structure and Ca^-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR
- Conformations of Vertebrate Striated Muscle Myosin Monomers in Equilibrium with Filaments
- Two Phosphorylations Specific to the Tali Region of the 204-kDa Heavy Chain Isoform of Porcine Aorta Smooth Muscle Myosin^1
- Asymmetric Photocross-Linking of Singly Phosphorylated Smooth Muscle Heavy Meromyosin
- Identification and Characterization of a Novel Calcineurin-Binding Protein in Scallop Testis
- IDENTIFICATION AS HEAT-SHOCK PROTEINS OF CALCIUM-DEPENDENT CALMODULIN BINDING PROTEIN FROM RAT SPERMATOGENIC CELLS(Developmental Biology)(Proceedings of the Seventy-Third Annual Meeting of the Zoological Society of Japan)
- Essential Light Chain Modulates Phosphorylation-Dependent Regulation of Smooth Muscle Myosin
- Functional Role of the C-Terminal Domain of Smooth Muscle Myosin Light Chain Kinase on the Phosphorylation of Smooth Muscle Myosin
- Two New Modes of Smooth Muscle Myosin Regulation by the Interaction between the Two Regulatory Light Chains, and by the S2 Domain
- Conformation,Filament Assembly,and Activity of Single-Headed Smooth Muscle Myosin
- Crosslinking of Telokin to Chicken Gizzard Smooth Muscle Myosin
- Evidence for Involvement of a 12-Residue Peptide Segment of the Heavy Chain in the Neck Region of Smooth Muscle Myosin in Formation of the 10S Conformation
- Molecular Cloning of cDNA Encoding Two Subunits of Calcineurin from Scallop Testis : Demonstration of Stage-Specific Expression during Maturation of the Testis
- Conformation and Activity of Smooth Muscle Myosin Probed by Various Essential light Chains
- Mapping phosphorylation site of the regulatory light chain in smooth muscle myosin by immuno-electron microscopy
- Binding of Myosin Subfragment 1 to Actin
- Mapping Myosin-Binding Sites on Actin Probed by Peptides That Inhibit Actomyosin Interaction
- A Novel Protein Phosphatase-1 Inhibitory Protein Potentated by Protein Kinase C. Isolation from Porcin Aorta Media and Characterization
- Identification of Trimeric Myosin Phosphatase ( PP1M ) as a Targer for a Novel PKC-Potentiated Protein Phosphatase-1 Inhibitory Protein ( CPI17 ) in Porcine Aorta Smooth Muscle
- Roles of calmodulin and calmodulin-binding proteins in synaptic vesicle recycling during regulated exocytosis at submicromolar Ca^ concentrations
- Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy
- Two New Modes of Smooth Muscle Myosin Regulation by the Interaction between the Two Regulatory Light Chains, and by the S2 Domain.