Localization of a new proteolytic site accessible in oxidized myosin rod

László Nyitray, Gábor Mócz, Miklós Bálint

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Abstract

We have compared the proteolysis pattern of reduced and oxidized myosin rods in which the five pairs of SH-groups were interchain crosslinked by employing CuCl2 or 5,5'-dithiobis-2-nitrobenzoate. In the tryptic digest of oxidized rod three new fragments appeared on SDS-polyacrylamide gel electrophoresis (chain masses of 100, 45, and 25 kDa). Based on the N-terminal sequences of the isolated peptides, it is concluded that oxidation creates a new cleavage site 102 residues away from the N-terminus of the rod, in the vicinity of one of the modified SH-groups (Cys-108). This observation indicates that S-S crosslinking of myosin rod leads to a local unfolding of the coiled-coil structure.

Original languageEnglish
Pages (from-to)353-356
Number of pages4
JournalFEBS letters
Volume181
Issue number2
DOIs
Publication statusPublished - Feb 25 1985

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Keywords

  • Coiled-coil structure
  • Disulfide crosslinking
  • Limited proteolysis
  • Myosin rod

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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