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Titolo:
THE STRUCTURE OF THE SARCOMERIC M-BAND - LOCALIZATION OF DEFINED DOMAINS OF MYOMESIN, M-PROTEIN, AND THE 250-KD CARBOXY-TERMINAL REGION OF TITIN BY IMMUNOELECTRON MICROSCOPY
Autore:
OBERMANN WMJ; GAUTEL M; STEINER F; VANDERVEN PFM; WEBER K; FURST DO;
Indirizzi:
UNIV POTSDAM,DEPT CELL BIOL,LENNESTR 7A D-14471 POTSDAM GERMANY UNIV POTSDAM,DEPT CELL BIOL D-14471 POTSDAM GERMANY MAX PLANCK INST BIOPHYS CHEM,DEPT BIOCHEM D-37077 GOTTINGEN GERMANY EUROPEAN MOL BIOL LAB,BIOL STRUCT & BIOCOMP PROGRAM D-69012 HEIDELBERG GERMANY
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 134, anno: 1996,
pagine: 1441 - 1453
SICI:
0021-9525(1996)134:6<1441:TSOTSM>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCLE C-PROTEIN; SKELETAL-MUSCLE; MONOCLONAL-ANTIBODIES; IMMUNOGLOBULIN SUPERFAMILY; DIFFERENTIAL EXPRESSION; PECTORAL MUSCLE; GLOBULAR HEAD; A-BAND; MYBP-C; CDNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
W.M.J. Obermann et al., "THE STRUCTURE OF THE SARCOMERIC M-BAND - LOCALIZATION OF DEFINED DOMAINS OF MYOMESIN, M-PROTEIN, AND THE 250-KD CARBOXY-TERMINAL REGION OF TITIN BY IMMUNOELECTRON MICROSCOPY", The Journal of cell biology, 134(6), 1996, pp. 1441-1453

Abstract

The M band of vertebrate cross-striated myofibrils has remained an enigmatic structure. In addition to myosin thick filaments, two major structural proteins, myomesin and M-protein, have been localized to the M band. Also, titin is expected to be anchored in this structure. To begin to understand the molecular layout of these three proteins, a panel of 16 polyclonal and monoclonal antibodies directed against unique epitopes of defined sequence was assembled, and immunoelectron microscopy was used to locate the position of the epitopes at the sarcomere level. The results allow the localization and orientation of defined domains of titin, myomesin, and M-protein at high resolution. The 250-kDcarboxy-terminal region of titin clearly enters the M band with the kinase domain situated similar to 52 nm from the central Mi-line. The positions of three additional epitopes are compatible with the view that the titin molecule reaches similar to 60 nm into the opposite sarcomere half. Myomesin also seems to bridge the central MI-line and is oriented parallel to the long axis of the myofibril. The neighboring molecules are oriented in an antiparallel and staggered fashion. The amino-terminal portion of the protein, known to contain a myosin binding site, seems to adopt a specific three-dimensional arrangement. While myomesin is present in both slow and fast fibers, M-protein is restrictedto fast fibers. It appears to be organized in a fundamentally different manner: the central portion of the polypeptide is around the MI-line, while the terminal epitopes seem to be arranged along thick filaments. This orientation fits the conspicuously stronger M1-lines in fast twitch fibers. Obvious implications of this model are discussed.

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Documento generato il 03/12/20 alle ore 15:45:58