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Protein machines and self assembly in muscle organization
Author(s) -
Barral José M.,
Epstein Henry F.
Publication year - 1999
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199910)21:10<813::aid-bies3>3.0.co;2-0
Subject(s) - muscle protein , microbiology and biotechnology , chemistry , computational biology , biology , anatomy , skeletal muscle
The remarkable order of striated muscle is the result of a complex series of protein interactions at different levels of organization. Within muscle, the thick filament and its major protein myosin are classical examples of functioning protein machines. Our understanding of the structure and assembly of thick filaments and their organization into the regular arrays of the A‐band has recently been enhanced by the application of biochemical, genetic, and structural approaches. Detailed studies of the thick filament backbone have shown that the myosins are organized into a tubular structure. Additional protein machines and specific myosin rod sequences have been identified that play significant roles in thick filament structure, assembly, and organization. These include intrinsic filament components, cross‐linking molecules of the M‐band and constituents of the membrane‐cytoskeleton system. Muscle organization is directed by the multistep actions of protein machines that take advantage of well‐established self‐assembly relationships. BioEssays 21:813–823, 1999. © 1999 John Wiley & Sons, Inc.