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, Rajini 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

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Cytochromes c1
Cytochromes c
Yeast
Lysine
Arginine
L-Lactate Dehydrogenase (Cytochrome)
Yeasts
Cytochrome-c Peroxidase
Mutagenesis
Gene encoding
Electron Transport Complex IV
Site-Directed Mutagenesis
Oligonucleotides
Saccharomyces cerevisiae
Proteins
Genes
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

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

In: Journal of Biological Chemistry, Vol. 262, No. 15, 25.05.1987, p. 7125-7131.

Research output: Contribution to journalArticle

Holzschu, D, Principio, L, Conklin, KT, Hickey, DR, 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, vol. 262, no. 15, pp. 7125-7131.
Holzschu, D. ; Principio, L. ; Conklin, K. T. ; Hickey, D. R. ; Short, J. ; Rao, Rajini ; McLendon, G. ; Sherman, F. / 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. In: Journal of Biological Chemistry. 1987 ; Vol. 262, No. 15. pp. 7125-7131.
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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.",
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AU - Principio, L.

AU - Conklin, K. T.

AU - Hickey, D. R.

AU - Short, J.

AU - Rao, Rajini

AU - McLendon, G.

AU - Sherman, F.

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AB - 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.

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