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Evidence that nebulin is a protein‐ruler in muscle thin filaments
Author(s) -
Labeit S.,
Gibson T.,
Lakey A.,
Leonard K.,
Zeviani M.,
Knight P.,
Wardale J.,
Trinick J.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80503-u
Subject(s) - nebulin , tropomyosin , actin , protein filament , myofibril , peptide sequence , biophysics , chemistry , biology , biochemistry , microbiology and biotechnology , sarcomere , gene , myocyte , titin
Partial amino acid sequence was obtained from the massive myofibrillar protein nebulin. This consists of repeating motifs of about 35 residues and super‐repeats of 7 × 35 = 245 residues. The repeat‐motifs are likely to be largely α‐helical and to interact with both actin and tropomyosin in thin filaments. Nebulin from different species was found to vary in size in proportion to filament length. The data are consistent with the proposal that nebulin acts as a protein‐ruler to regulate precise thin filament assembly.