Elsevier

FEBS Letters

Volume 281, Issues 1–2, 9 April 1991, Pages 23-26
FEBS Letters

Rabbit skeletal muscle myosin unfolded carboxyl-terminus and its role in molecular assembly

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Abstract

We have expressed in E. coli segments of the rod portion of rabbit skeletal fast muscle myosin and compared physical properties of two different species, LMM-30 and LMM-30C′. LMM-30 consists of 263 amino acids including the original C-terminus of myosin heavy chain. LMM-30C′ is colinear with LMM-30, but is devoid of 17 residues at the C-terminus. 1H NMR spectroscopy indicates that the C-terminus of LMM-30, but not of LMM30C′ is unfolded and freely mobile. Furthermore, the present results show that the unfolded C-terminus is essential for molecular assembly of LMM-30; at pH 8.0 LMM-30, but not LMM-30C′, formed aggregates upon decreasing the ionic strength.

Keywords

Myosin
α-Helical coiled-coil
Self-assembly
Recombinant DNA technique
Nuclear magnetic resonance

Abbreviations

LMM
light meromyosin
NMR
nuclear magnetic resonance

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