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Titolo:
THE ELASTIC I-BAND REGION OF TITIN IS ASSEMBLED IN A MODULAR FASHION BY WEAKLY INTERACTING IG-LIKE DOMAINS
Autore:
POLITOU AS; GAUTEL M; IMPROTA S; VANGELISTA L; PASTORE A;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1 D-69117 HEIDELBERG GERMANY
Titolo Testata:
Journal of Molecular Biology
fascicolo: 4, volume: 255, anno: 1996,
pagine: 604 - 616
SICI:
0022-2836(1996)255:4<604:TEIROT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOGLYCERATE KINASE; CRYSTAL-STRUCTURE; SKELETAL-MUSCLE; MOLECULAR-BASIS; PROTEIN; FILAMENTS; DENATURATION; COOPERATIVITY; CONNECTIN; SYSTEM;
Keywords:
CONNECTIN; ELASTICITY; INTERFACE; MODULE; MUSCLE; UNFOLDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
A.S. Politou et al., "THE ELASTIC I-BAND REGION OF TITIN IS ASSEMBLED IN A MODULAR FASHION BY WEAKLY INTERACTING IG-LIKE DOMAINS", Journal of Molecular Biology, 255(4), 1996, pp. 604-616

Abstract

The vertebrate striated muscle protein titin is thought to play a critical role in myofibril assembly and passive tension. The recently determined complete primary structure of titin revealed a modular architecture that opens the way to a structural characterisation and the understanding of essential properties of this molecule through dissection into units that are structurally and/or functionally relevant. To understand the assembly process of titin, and ultimately the molecular basis of its elastic behaviour, we studied the thermodynamic properties of module pairs, the smallest structural unit that includes a module-module interface. Thus, selected module pairs and their component singlemodules from the I-band part of the titin molecule were expressed in Escherichia coli and their heat-induced and denaturant-induced unfolding was investigated. with a combination of techniques (circular dichroism, fluorescence spectroscopy and nuclear magnetic resonance). The stabilities of single modules and pairs were determined from denaturation experiments. The module interface was also modelled on the basis of the sequence alignment of all similar to 40 immunoglobulin like modules from the I-band and the known structure of one of them. Our results show that all modules and module pairs examined are independently folded in solution. When covalently linked, although weakly interacting, they still behave as autonomous co-operative units upon unfolding. These observations lead us to suggest that folding of titin in vitro is a hierarchical event and that weak interactions between its adjacent modules must only partly account for its presumed elastic function. (C) 1996 Academic Press Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 20:38:03