Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments.

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Abstract Text:

T Takahashi,C Fukukawa,C Naraoka,T Katoh,M Yazawa,

Porcine cardiac myosin monomers in equilibrium with filaments under physiological conditions were observed to have two conformations, extended and folded forms, upon electron microscopy and gel filtration HPLC. The conformational state was independent of ATP and the phosphorylation of regulatory light chain. The folded monomers of cardiac myosin were mainly in an open conformation with only one bend in the tail, and may not trap the hydrolysis products of ATP, as assessed by single turnover experiments. These properties are similar to those of the folded monomers of rabbit skeletal myosin [Katoh, T., Konishi, K., and Yazawa, M. (1998) J. Biol. Chem. 273, 11436-11439]. The conformational states of skeletal and cardiac myosin monomers were not affected by pH between 7.0 and 8.5. Although significant disassembly of filaments and thus an increase in the monomer concentration were observed with an increase in pH. The results indicate that the pH-dependent change in filament assembly is due to a shift of equilibrium between the filaments and extended monomers toward filament disassembly. The Mg2+-ATPase activity of these myosin monomers decreased with a decrease in the salt concentration below approximately 0.1 M, suggestive of the formation of a closed conformation similar to the conformation of 10S smooth myosin. The results suggest that the conformational change from the extended to the folded form is a common property of various myosin IIs.

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Publishing Authors By Initials

T Takahashi,C Fukukawa,C Naraoka,T Katoh,M Yazawa,

For similar animals: chordata: vertebrates research abstracts see: animals: chordata: vertebrates research

PUBMED ID PMID:

MEDLINE DATE:

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 126

Page Numbers: 34-40

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1999

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Keywords Mesh Terms:

KEYWORDS: Vertebrates

MESH TERMS: metabolism

Chemical & Substance for Abstract: Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments.

AFFILIATION: Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments Related Publications

• Anti-hyperglycemic activity of kiwifruit leaf (Actinidia deliciosa) in mice.
• Asymmetric photocross-linking of singly phosphorylated smooth muscle heavy meromyosin.
• Biosynthesis of the blood group P antigen-like GalNAc beta 1-->3Gal beta 1-->4GlcNAc/Glc structure: a novel N-acetylgalactosaminyltransferase in human blood plasma.
• Characteristic thickened cell walls of the bracts of the 'eternal flower' Helichrysum bracteatum.
• Conformation, filament assembly, and activity of single-headed smooth muscle myosin.
• Conformations of vertebrate striated muscle myosin monomers in equilibrium with filaments.
• Crosslinking of telokin to chicken gizzard smooth muscle myosin.
• Electrocochleography in experimental endolymphatic hydrops.
• Essential light chain modulates phosphorylation-dependent regulation of smooth muscle myosin.
• Identification and characterization of a novel calcineurin-binding protein in scallop testis.
• Identification of trimeric myosin phosphatase (PP1M) as a target for a novel PKC-potentiated protein phosphatase-1 inhibitory protein (CPI17) in porcine aorta smooth muscle.
• Isolation and characterization of a subfragment of myosin A.
• Low molecular weight components (g-chains) of myosin from rabbit skeletal muscle. Separation, amino acid compositions and contents in myosin.
• Molecular cloning of cDNA encoding two subunits of calcineurin from scallop testis: demonstration of stage-specific expression during maturation of the testis.
• New Phospholipase A(1)-producing Bacteria from a Marine Fish.
• Properties of calcium-dependent regulatory proteins from fungi and yeast.
• Rebound phenomenon in glycerol test.
• Suppressive effects of Anoectochilus formosanus extract on osteoclast formation in vitro and bone resorption in vivo.
• Swimming test for evaluating vestibular function in guinea pigs.
• [Mediastinal parathyroid cyst]
• [Successful perioperative management with non-invasive positive pressure ventilation in muscular dystrophy with thymoma; report of a case]