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Titolo:
TITIN DOMAIN PATTERNS CORRELATE WITH THE AXIAL DISPOSITION OF MYOSIN AT THE END OF THE THICK FILAMENT
Autore:
BENNETT PM; GAUTEL M;
Indirizzi:
UNIV LONDON KINGS COLL,MRC,MUSCLE & CELL MOTIL UNIT,RANDALL INST,26-29 DRURY LANE LONDON WC2 B5RL ENGLAND EUROPEAN MOLEC BIOL LAB D-69126 HEIDELBERG GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 5, volume: 259, anno: 1996,
pagine: 896 - 903
SICI:
0022-2836(1996)259:5<896:TDPCWT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
VERTEBRATE SKELETAL-MUSCLE; IMMUNOELECTRON MICROSCOPY; ELASTIC PROTEIN; STRIATED-MUSCLE; MONOCLONAL-ANTIBODIES; CONNECTIN FILAMENTS; MYASTHENIA-GRAVIS; Z-LINE; FROG; BAND;
Keywords:
TITIN/CONNECTIN; MYOSIN; SARCOMERIC ASSEMBLY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
P.M. Bennett e M. Gautel, "TITIN DOMAIN PATTERNS CORRELATE WITH THE AXIAL DISPOSITION OF MYOSIN AT THE END OF THE THICK FILAMENT", Journal of Molecular Biology, 259(5), 1996, pp. 896-903

Abstract

Titin has been suggested to act as a molecular ruler for the precise assembly of thick filaments in vertebrate striated muscle. To investigate the correlation of titin domain patterns with the architecture of the thick filament at its end, we have investigated the axial positionof titin epitopes at the thick-filament/I-band junction. Antibodies against immunoglobin (Ig) domains N and C-terminal to the unique block of six fibronectin-3 (fn3) domains in this region were used. The distance between these epitopes confirms the idea that titin is laid out linearly along the thick filament with each domain measuring about 1 nm in length. Our data demonstrate that the gap of myosin crossbridges near the end of the thick filament closely correlates with the stretch of six fn3 domains, and that the last two crossbridges are at the levelof the first two groups of fn3 domains which were previously assignedto the I-band. We conclude that the pattern of groups of fn3 domains reflects the arrangement of the myosin heads, at least at the end of the A-band. It seems likely that an alteration in the interaction between myosin and the titin fn3 domains towards the end of the thick filament is important for the formation of the crossbridge gap and thus thetermination of the thick filament. (C) 1996 Academic Press Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:09:17