Replacement of the invariant lysine 77 by arginine in yeast iso-1-cytochrome c results in enhanced and normal activities in vitro and in vivo.

D. Holzschu, L. Principio, K. T. Conklin, D. R. Hickey, J. Short, R. Rao, G. McLendon, F. Sherman

Research output: Contribution to journalArticle

Abstract

Oligonucleotide-directed mutagenesis of the yeast Saccharomyces cerevisiae was used to generate an abnormal iso-1-cytochrome c having an Arg-77 replacement of the normal Lys-77; this Lys-77 residue is evolutionarily conserved in most eukaryotic cytochromes c and is trimethylated in fungal and plant cytochromes c. Examination of strains having a single chromosomal copy of the gene encoding the Arg-77 protein indicated that the altered protein was synthesized at the normal rate and that it had normal or near normal activity in vivo. Examination of enzymatic activities in vitro with cytochrome b2, cytochrome c peroxidase, and cytochrome c oxidase indicated that the altered iso-1-cytochrome c has equal or enhanced catalytic efficiencies. Thus, replacement of the evolutionarily conserved residue Lys-77 produces no or only minor effects both in vivo and in vitro.

Original languageEnglish (US)
Pages (from-to)7125-7131
Number of pages7
JournalJournal of Biological Chemistry
Volume262
Issue number15
StatePublished - May 25 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Holzschu, D., Principio, L., Conklin, K. T., Hickey, D. R., Short, J., Rao, R., McLendon, G., & Sherman, F. (1987). Replacement of the invariant lysine 77 by arginine in yeast iso-1-cytochrome c results in enhanced and normal activities in vitro and in vivo. Journal of Biological Chemistry, 262(15), 7125-7131.