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Titolo:
Molecular evolution of immunoglobulin and fibronectin domains in titin andrelated muscle proteins
Autore:
Kenny, PA; Liston, EM; Higgins, DG;
Indirizzi:
Natl Univ Ireland Univ Coll Cork, Dept Biochem, Cork, Ireland Natl Univ Ireland Univ Coll Cork Cork Ireland pt Biochem, Cork, Ireland
Titolo Testata:
GENE
fascicolo: 1, volume: 232, anno: 1999,
pagine: 11 - 23
SICI:
0378-1119(19990517)232:1<11:MEOIAF>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGHT CHAIN KINASE; SARCOMERIC M-BAND; C C-PROTEIN; MYBP-C; CAENORHABDITIS-ELEGANS; CARBOXYL-TERMINUS; STRUCTURAL BASIS; MODULAR PROTEIN; SKELETAL-MUSCLE; I-BAND;
Keywords:
F12F3.2; fibronectin type III domain; immunoglobulin I set domain; phylogenetic analysis; projectin; twitchin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Kenny, PA Inst Canc Res, Chester Beatty Labs, 237 Fulham Rd, London SW3 6JB, England Inst Canc Res 237 Fulham Rd London England SW3 6JB 6JB, England
Citazione:
P.A. Kenny et al., "Molecular evolution of immunoglobulin and fibronectin domains in titin andrelated muscle proteins", GENE, 232(1), 1999, pp. 11-23

Abstract

The family of regulatory and structural muscle proteins, which includes the giant kinases titin, twitchin and projectin, has sequences composed predominantly of serially linked immunoglobulin I set (Ig) and fibronectin type III (FN3) domains. This paper explores the evolutionary relationships between 16 members of this family. In titin, groups of Ig and FN3 domains are arranged in a regularly repeating pattern of seven and 11 domains. The Ii-domain super-repeat has its origins in the seven-domain super-repeat and a model for the duplications which gave rise to this super-repeat is proposed. Asuper-repeat composed solely of immunoglobulin domains is found in the skeletal muscle isoform of titin. Twitchin and projectin, which are presumed to be orthologs, have undergone significant insertion/deletion of domains since their divergence. The common ancestry of myomesin, skelemin and M-protein is shown. The relationship between myosin binding proteins (MyBPs) C andH is confirmed, and MyBP-H is proposed to have given rise to MyBP-C by theacquisition of some titin domains. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 18:31:07