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Essential role of the HMG domain in the function of yeast mitochondrial histone HM: functional complementation of HM by the nuclear nonhistone protein NHP6A.
Kao, L R; Megraw, T L; Chae, C B.
Afiliación
  • Kao LR; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill 27599-7260.
Proc Natl Acad Sci U S A ; 90(12): 5598-602, 1993 Jun 15.
Article en En | MEDLINE | ID: mdl-8516306
The yeast mitochondrial histone protein HM is required for maintenance of the mitochondrial genome, and disruption of the gene encoding HM (HIM1/ABF2) results in formation of a respiration-deficient petite mutant phenotype. HM contains two homologous regions, which share sequence similarity with the eukaryotic nuclear nonhistone protein, HMG-1. Experiments with various deletion mutants of HM show that a single HMG domain of HM is functional and can restore respiration competency to cells that lack HM protein (him1 mutant cells). The gene encoding the putative yeast nuclear HMG-1 homolog, the NHP6A protein, can functionally complement the him1 mutation. These results suggest that the HMG domain is the basic unit for the function of HM in mitochondria and that the function of HMG-1 proteins in the nucleus and HM in the mitochondrion may be equivalent.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas de Transporte de Monosacáridos / Proteínas del Grupo de Alta Movilidad / Transportadoras de Casetes de Unión a ATP / Proteínas de Escherichia coli / Proteínas de Unión al ADN / Mitocondrias Límite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1993 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Proteínas de Transporte de Monosacáridos / Proteínas del Grupo de Alta Movilidad / Transportadoras de Casetes de Unión a ATP / Proteínas de Escherichia coli / Proteínas de Unión al ADN / Mitocondrias Límite: Animals Idioma: En Revista: Proc Natl Acad Sci U S A Año: 1993 Tipo del documento: Article