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Nebulin as a giant actin‐binding template protein in skeletal muscle sarcomere Interaction of actin and cloned human nebulin fragments
Author(s) -
Jin Jian-Ping,
Wang Kuan
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)80366-b
Subject(s) - nebulin , sarcomere , actin , biology , skeletal muscle , actin binding protein , microbiology and biotechnology , biochemistry , myocyte , titin , actin cytoskeleton , anatomy , cytoskeleton , cell
Nebulin is a family of giant sarcomere matrix proteins of 6OO–900 kDa in most vertebrate skeletal muscles. Recent sequence analysis suggests that human nebulin is mainly composed of a large number (> 200) of conserved repeats of ∼ 35 residues. Two cloned nebulin fragments, consisting of 6 and 8 of the repeats, have been expressed in E. coli using the pET3d vector. Both F‐actin cosedimentation and solid‐phase binding assays demonstrated a specific binding of these nebulin fragments to actin. This finding suggests that nebulin is a giant protein which binds actin at multiple sites in a template‐manner. The presence of an actin‐binding template protein in the skeletal muscle sarcomere may have significant implications in the assembly and function of the contractile apparatus.