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

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 LMM-30C' 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Maeda K,Rösch A,Maéda Y,Kalbitzer HR,Wittinghofer A

doi

10.1016/0014-5793(91)80349-8

subject

Has Abstract

pub_date

1991-04-09 00:00:00

pages

23-6

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80349-8

journal_volume

281

pub_type

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