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Titolo:
A CALMODULIN-BINDING SEQUENCE IN THE C-TERMINUS OF HUMAN CARDIAC TITIN KINASE
Autore:
GAUTEL M; MORELLI MAC; PFUHL M; MOTTA A; PASTORE A;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1 D-69012 HEIDELBERG GERMANY EUROPEAN MOLEC BIOL LAB D-69012 HEIDELBERG GERMANY UNIV BASILICATA,DIPARTIMENTO CHIM I-85100 POTENZA ITALY CNR,IST CHIM MOLEC INTERESSE BIOL ARCO ITALY
Titolo Testata:
European journal of biochemistry
fascicolo: 2, volume: 230, anno: 1995,
pagine: 752 - 759
SICI:
0014-2956(1995)230:2<752:ACSITC>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGHT-CHAIN KINASE; INTRASTERIC REGULATION; MULTIDIMENSIONAL NMR; PEPTIDE COMPLEX; ACTIVE-SITE; MYOSIN; DOMAIN; PURIFICATION; RECOGNITION; PROTEINS;
Keywords:
MUSCLES; TITIN; CONNECTIN; PROTEIN KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
M. Gautel et al., "A CALMODULIN-BINDING SEQUENCE IN THE C-TERMINUS OF HUMAN CARDIAC TITIN KINASE", European journal of biochemistry, 230(2), 1995, pp. 752-759

Abstract

The giant muscle proteins of the titin family, which are specific forthe striated muscles of vertebrates and invertebrates, contain as a common feature a catalytic protein kinase domain of so far unclear function and regulation, In myosin light chain kinase, a family evolutionarily related to titin, kinase regulation is achieved by calmodulin binding to a region of the kinase C-terminus which bears similarity to the substrate. A calmodulin-binding sequence has also been identified inthe C-terminus of the Aplysia twitchin kinase. In analogy, we identified a putative calmodulin-binding site in the titin kinase C-terminal sequence. The expressed catalytic domain itself and a series of synthetic peptides from this region wore tested for their ability to bind calmodulin. Biochemical data indicate that titin kinase as well as peptides from its C-terminus bind to calmodulin in an equimolar complex in the presence of calcium. The interaction of truncated peptides with calmodulin is, however, weaker than that of myosin light chain kinase. Nuclear magnetic resonance studies showed that these peptides have a tendency to adopt alpha-helical conformations in solution. Helicity increases upon binding of calmodulin in a calcium-dependent fashion, as judged by circular dichroism spectra. We, therefore, propose that this calmodulin-binding region of titin could play a regulatory role for theenzyme, the substrate of which still remains to be identified.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 14:23:11