Nom du corpus

Corpus Systématique Animale

Titre du document

Essential and regulatory light chains of Placopecten striated and catch muscle myosins

Lien vers le document
Éditeur
Springer (journals)
Langue(s) du document
Anglais
Type de document
Research-article
Nom du fichier dans la ressource
Mollusques_v2b_00898
Auteur(s)
  • Cynthia L. Perreault-Micale 1
  • Ágnes Jancsó 1
  • Andrew G. Szent-Györgyi 1
Affiliation(s)
  • 1) Department of Biology, Brandeis University, 02254-9110, Waltham, MA, USA
Résumé

ATPase activities of molluscan adductor muscle myosins show both muscle and species specific differences: ATPase activity of catch muscle myosin is lower than that of phasic muscle myosin; a 4–5-fold difference exists between the activities of phasic striated muscle myosins from the bay scallop (Argopecten irradians) and sea scallop (Placopecten magellanicus). To characterize the light chains of these myosins we determined the cDNA sequences of the essential light chains and the regulatory light chains from Placopecten striated and catch muscle. The nucleotide sequences of the essential light chains from Placopecten striated and catch muscle myosins are identical and show 94% identity and 98% homology to the Argopecten essential light chain indicating that the tissue and species specific differences in ATPase activities are not due to the essential light chain. We identified three regulatory light chain isoforms, one from striated and two from catch muscle. Sequence differences were restricted to nucleotides encoding some of the N-terminal 52 amino acids. The three recombinant Placopecten regulatory light chain isoforms and the Argopecten regulatory light chain were incorporated into hybrid myosins that contained the essential light chain and heavy chain from Placopecten striated, Placopecten catch, or Argopecten striated muscle. Measurement of the ATPase activities of these hybrids indicates clearly that it is the myosin heavy chain and not the regulatory light chains that are responsible for the muscle and species specific differences in enzymatic activities. Analysis of genomic DNA indicated that these regulatory light chain isoforms are products of a single regulatory light chain gene that is alternatively spliced in the 5? region only.

Catégories Science-Metrix
  • 1 - health sciences
  • 2 - biomedical research
  • 3 - physiology
Catégories INIST
  • 1 - sciences appliquees, technologies et medecines
  • 2 - sciences biologiques et medicales
  • 3 - sciences biologiques fondamentales et appliquees. psychologie
Catégories Scopus
  • 1 - Life Sciences ; 2 - Biochemistry, Genetics and Molecular Biology ; 3 - Cell Biology
  • 1 - Life Sciences ; 2 - Biochemistry, Genetics and Molecular Biology ; 3 - Biochemistry
  • 1 - Life Sciences ; 2 - Biochemistry, Genetics and Molecular Biology ; 3 - Physiology
Catégories WoS
  • 1 - science ; 2 - cell biology
Identifiant ISTEX
E1723DCC25530F283C056A8CED63ED00D4095236
Revue

Journal of Muscle Research & Cell Motility

Année de publication
1996
Présence de XML structuré
Non
Version PDF
1.3
Score qualité du texte
10
Sous-corpus
  • Mollusques
Type de publication
Journal
ark:/67375/1BB-D0N5S43N-9
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