Processing of mitochondrial precursor proteins. 1991

M Arretz, and H Schneider, and U Wienhues, and W Neupert
Institut für Physiologische Chemie, Universität München, FRG.

The mitochondrial processing enzyme consists of two components, the mitochondrial processing peptidase (MPP) and processing enhancing protein (PEP). MPP and PEP act cooperatively in proteolytic processing of mitochondrial precursor proteins. Most of the mitochondrial precursors possess aminoterminal presequences (also called "targeting sequences" or "signal sequences"), that do not display a common motif and that show only limited similarities of the cleavage sites. The mitochondrial processing peptidase is a metal-dependent endoprotease, sensitive to sulfhydryl-modifying reagents and appears to belong to a new class of proteases. MPP and PEP, together with the core 1 and core 2 proteins of the respiratory complex III, form a new protein family.

UI MeSH Term Description Entries
D008666 Metalloendopeptidases ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism. Metallo-Endoproteinases,Metalloendopeptidase
D008928 Mitochondria Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed) Mitochondrial Contraction,Mitochondrion,Contraction, Mitochondrial,Contractions, Mitochondrial,Mitochondrial Contractions
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009492 Neurospora crassa A species of ascomycetous fungi of the family Sordariaceae, order SORDARIALES, much used in biochemical, genetic, and physiologic studies. Chrysonilia crassa
D011498 Protein Precursors Precursors, Protein
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D000096122 Mitochondrial Processing Peptidase A hetero-dimeric protein consisting of two subunits, alpha and beta, which are referred to as PMPCA and PMPCB in humans. It plays an essential role in removing the N-terminal targeting peptidase from precursor proteins imported into the mitochondria. Matrix Processing Peptidase,Mitochondrial Processing Protease,alpha-MPP,beta-MPP,Peptidase, Matrix Processing,Peptidase, Mitochondrial Processing,Processing Peptidase, Matrix,Processing Peptidase, Mitochondrial,Processing Protease, Mitochondrial,Protease, Mitochondrial Processing,alpha MPP,beta MPP
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker

Related Publications

M Arretz, and H Schneider, and U Wienhues, and W Neupert
November 1999, Biochemical and biophysical research communications,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
February 1986, Biochemical and biophysical research communications,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
June 1989, The Journal of biological chemistry,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
October 1994, The Journal of biological chemistry,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
February 1991, Plant molecular biology,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
December 1989, Archives of biochemistry and biophysics,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
April 1998, The Journal of biological chemistry,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
January 1990, Biochemistry and cell biology = Biochimie et biologie cellulaire,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
April 1994, European journal of biochemistry,
M Arretz, and H Schneider, and U Wienhues, and W Neupert
June 1990, Archives of biochemistry and biophysics,
Copied contents to your clipboard!