Rabbit skeletal muscle myosin. Unfolded carboxyl-terminus and its role in molecular assembly.
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.
Maeda
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K
Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.
Rösch
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Maéda
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Kalbitzer
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Wittinghofer
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005822:Genetic Vectors; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000737:chemistry / Q000235:genetics*; D015345:Oligonucleotide Probes; D011487:Protein Conformation; D011817:Rabbits; D012995:Solubility
D015345:Oligonucleotide Probes; D009218:Myosins