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Titolo:
A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila
Autore:
Naimi, B; Harrison, A; Cummins, M; Nongthomba, U; Clark, S; Canal, I; Ferrus, A; Sparrow, JC;
Indirizzi:
Univ York, Dept Biol, York YO10 5YW, N Yorkshire, England Univ York York N Yorkshire England YO10 5YW O10 5YW, N Yorkshire, England CSIC, Inst Cajal, E-28002 Madrid, Spain CSIC Madrid Spain E-28002CSIC, Inst Cajal, E-28002 Madrid, Spain
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 5, volume: 12, anno: 2001,
pagine: 1529 - 1539
SICI:
1059-1524(200105)12:5<1529:ATMSAT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
FLIGHT-MUSCLE; HYPERTROPHIC CARDIOMYOPATHY; CAENORHABDITIS-ELEGANS; ACTIN-TROPOMYOSIN; ALPHA-TROPOMYOSIN; SKELETAL-MUSCLE; CO-CRYSTALS; MELANOGASTER; GENE; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Sparrow, JC Univ York, Dept Biol, York YO10 5YW, N Yorkshire, England UnivYork York N Yorkshire England YO10 5YW orkshire, England
Citazione:
B. Naimi et al., "A tropomyosin-2 mutation suppresses a troponin I myopathy in Drosophila", MOL BIOL CE, 12(5), 2001, pp. 1529-1539

Abstract

A suppressor mutation, D53, of the held-up(2) allele of the Drosophila melanogaster Troponin I (wupA) gene is described. D53, a missense mutation, S185F, of the tropomyosin-2, Tm2, gene fully suppresses all the phenotypic effects of held-up(2), including the destructive hypercontraction of the indirect flight muscles (IFMs), a lack of jumping, the progressive myopathy of the walking muscles, and reductions in larval crawling and feeding behavior. The suppressor restores normal function of the IFMs, but flight ability decreases with age and correlates with an unusual, progressive structural collapse of the myofibrillar lattice starting at the center. The S185F substitution in Tm2 is close to a troponin T binding site on tropomyosin. Models to explain suppression by D53, derived from current knowledge of the vertebrate troponin-tropomyosin complex structure and functions, are discussed. The effects of S185F are compared with those of two mutations in residues 175 and 180 of human alpha -tropomyosin 1 which cause familial hypertrophic cardiomyopathy (HCM).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 01:54:20