| A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing. | |
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MedLine Citation:
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PMID: 7907589 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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N-Acetylglutamate kinase (AGK) and N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) function as two separate mitochondrial enzymes, but are encoded by a single nuclear gene in several fungi. The Neurospora crassa arg-6 gene encoding these enzymes has been cloned and sequenced, and the enzymes responsible for processing the polyprotein precursor have been identified. The 871-amino acid precursor contains a normal N-terminal mitochondrial targeting sequence, an internal connecting region (approximately 200 amino acids) upstream of the distal reductase domain, and coding regions with N-terminal amino acid sequences identical with those of purified N-acetylglutamate kinase and N-acetyl-gamma-glutamyl-phosphate reductase. Sequence comparisons of the coding regions indicate high levels of conservation between prokaryotic and fungal proteins. Regions suggesting ancestral relationships to N-acetylglutamate synthase and aspartate beta-semialdehyde dehydrogenase have been identified. Both the N-terminal targeting sequence and the connecting region contain consensus sites for cleavage by the mitochondrial processing peptidase and processing enhancing protein. In vitro processing assays with intact mitochondria, solubilized mitochondria, and purified enzymes have shown that the mitochondrial processing peptidase and processing enhancing protein cleave not only the N-terminal mitochondrial targeting sequence but also process the polyprotein precursor into the two mature enzymes. |
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Authors:
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S F Gessert; J H Kim; F E Nargang; R L Weiss |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 269 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1994 Mar |
Date Detail:
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Created Date: 1994-04-18 Completed Date: 1994-04-18 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 8189-203 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry, University of California, Los Angeles 90024-1569. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/L27746 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aldehyde Oxidoreductases
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biosynthesis*,
genetics Amino Acid Sequence Base Sequence Chromosome Mapping Chromosomes, Fungal Cloning, Molecular Conserved Sequence Cosmids Enzyme Precursors / genetics, metabolism* Escherichia coli / enzymology, genetics Evolution Genes, Fungal* Mitochondria / enzymology* Molecular Sequence Data Neurospora crassa / enzymology*, genetics* Phosphotransferases (Carboxyl Group Acceptor) / biosynthesis*, genetics Plasmids Polymorphism, Restriction Fragment Length Protein Biosynthesis Protein Processing, Post-Translational* Restriction Mapping Sequence Homology, Amino Acid Transcription, Genetic Transformation, Genetic |
| Grant Support | |
ID/Acronym/Agency:
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GM36552/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Enzyme Precursors; EC 1.2.-/Aldehyde Oxidoreductases; EC 1.2.1.38/N-acetyl-gamma-glutamyl-phosphate reductase; EC 2.7.2.-/Phosphotransferases (Carboxyl Group Acceptor); EC 2.7.2.8/acetylglutamate kinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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