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Rabbit skeletal muscle myosin unfolded carboxyl‐terminus and its role in molecular assembly
Author(s) -
Maeda Kayo,
Rösch Andrea,
Maéda Yuichiro,
Kalbitzer Hans Robert,
Wittinghofer Alfred
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)80349-8
Subject(s) - myosin , skeletal muscle , chemistry , microbiology and biotechnology , biophysics , biochemistry , biology , anatomy
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. 1 H 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.