Nebulin as a giant actin‐binding template protein in skeletal muscle sarcomere Interaction of actin and cloned human nebulin fragments

FEBS Letters

Jin, Jian-Ping¹  Wang, Kuan¹ 

[1] Clayton Foundation Biochemical Institute, Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA

关键词: Nebulin;    Actin-binding protein;    Muscle thin filament;    cDNA expression in E. Coli;    ELISA;   

DOI  :  10.1016/0014-5793(91)80366-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown