Literature DB >> 7926051

Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function.

R Tauer1, G Mannhaupt, R Schnall, A Pajic, T Langer, H Feldmann.   

Abstract

The yeast gene, YTA10, encodes a member of a novel family of putative ATPases. Yta10p, as deduced from the nucleotide sequence, is 761 amino acids in length (predicted molecular mass 84.5 kDa). The amino acid sequence of Yta10p exhibits high similarity to two other yeast proteins, Yta11 and Yta12, and to E. coli FtsH. Several features of Yta10p are compatible with its localization in mitochondria. We report here that Yta10p is a yeast mitochondrial protein and that import is dependent on a membrane potential and accompanied by processing to a protein of approximately 73 kDa. Disruption of YTA10 leads to a nuclear petite phenotype and to a loss of respiratory competence, as shown by spectrophotometric measurement of the activities of respiratory complexes I-III and IV, respectively. These findings together with the high similarity of Yta10p to several ATP-dependent proteases suggest that Yta10p is a mitochondrial component involved, directly or indirectly, in the correct assembly and/or maintenance of active respiratory complexes.

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Year:  1994        PMID: 7926051     DOI: 10.1016/0014-5793(94)01045-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  18 in total

1.  Two ftsH-family genes encoded in the nuclear and chloroplast genomes of the primitive red alga Cyanidioschyzon merolae.

Authors:  R Itoh; H Takano; N Ohta; S Miyagishima; H Kuroiwa; T Kuroiwa
Journal:  Plant Mol Biol       Date:  1999-10       Impact factor: 4.076

2.  The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria.

Authors:  L van Dyck; W Neupert; T Langer
Journal:  Genes Dev       Date:  1998-05-15       Impact factor: 11.361

3.  The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease.

Authors:  H Arlt; G Steglich; R Perryman; B Guiard; W Neupert; T Langer
Journal:  EMBO J       Date:  1998-08-17       Impact factor: 11.598

4.  AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.

Authors:  K Leonhard; J M Herrmann; R A Stuart; G Mannhaupt; W Neupert; T Langer
Journal:  EMBO J       Date:  1996-08-15       Impact factor: 11.598

Review 5.  Regulated protein degradation in mitochondria.

Authors:  T Langer; W Neupert
Journal:  Experientia       Date:  1996-12-15

6.  Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria.

Authors:  G Steglich; W Neupert; T Langer
Journal:  Mol Cell Biol       Date:  1999-05       Impact factor: 4.272

7.  Diminished degradation of yeast cytochrome c by interactions with its physiological partners.

Authors:  D A Pearce; F Sherman
Journal:  Proc Natl Acad Sci U S A       Date:  1995-04-25       Impact factor: 11.205

8.  Peripheral mitochondrial inner membrane protein, Mss2p, required for export of the mitochondrially coded Cox2p C tail in Saccharomyces cerevisiae.

Authors:  S A Broadley; C M Demlow; T D Fox
Journal:  Mol Cell Biol       Date:  2001-11       Impact factor: 4.272

9.  The sorting of mitochondrial DNA and mitochondrial proteins in zygotes: preferential transmission of mitochondrial DNA to the medial bud.

Authors:  K Okamoto; P S Perlman; R A Butow
Journal:  J Cell Biol       Date:  1998-08-10       Impact factor: 10.539

10.  Sequential processing of the Toxoplasma apicoplast membrane protein FtsH1 in topologically distinct domains during intracellular trafficking.

Authors:  Anuradha Karnataki; Amy E DeRocher; Jean E Feagin; Marilyn Parsons
Journal:  Mol Biochem Parasitol       Date:  2009-03-21       Impact factor: 1.759

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