Mammalian Mitochondrial Intermediate Peptidase: Structure/Function Analysis of a New Homologue from Schizophyllum commune and Relationship to Thimet Oligopeptidases

Mitochondrial intermediate peptidase (MIP) is a component of the mitochondrial protein import machinery required for maturation of nuclear-encoded precursor proteins targeted to the mitochondrial matrix or inner membrane. We previously characterized this enzyme in rat (RMIP) and Saccharomyces cerevi...

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Bibliographic Details
Published in:	Genomics (San Diego, Calif.) Vol. 28; no. 3; pp. 450 - 461
Main Authors:	Isaya, Grazia, Sakati, Wayne R., Rollins, Robert A., Shen, Guang P., Hanson, Lee Q., Ullrich, Robert C., Novotny, Charles P.
Format:	Journal Article
Language:	English
Published:	San Diego, CA Elsevier Inc 10-08-1995 Elsevier
Subjects:	ADN Amino Acid Sequence AMINO ACID SEQUENCES Animals Base Sequence Biological and medical sciences CHEMICAL COMPOSITION COMPARISONS COMPLEMENTARY DNA COMPOSICION QUIMICA COMPOSITION CHIMIQUE Conserved Sequence DNA DNA, Fungal EXONS Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism genbank/l43072 GENE GENES Genes. Genome INTRONS Mammals Metalloendopeptidases - chemistry Metalloendopeptidases - genetics Metalloendopeptidases - metabolism MITOCHONDRIA MITOCHONDRIE MITOCONDRIA Molecular and cellular biology Molecular genetics Molecular Sequence Data Mutation NUCLEOTIDE SEQUENCE PEPTIDASAS PEPTIDASE PEPTIDASES Phenotype Protein Precursors RAT RATA RATS SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Schizophyllum - enzymology SCHIZOPHYLLUM COMMUNE SECUENCIA NUCLEICA Sequence Homology, Amino Acid SEQUENCE NUCLEIQUE smip gene STRUCTURAL GENES Intracellular transport Import Nucleotide sequence Enzyme Gene product Basidiomycetes Homology Nucleocytoplasmic interaction Gene expression Fungi Proteins Mitochondria Schizophyllum commune Enzymatic activity Complementary DNA Hydrolases Proteinases Thallophyta
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Summary:	Mitochondrial intermediate peptidase (MIP) is a component of the mitochondrial protein import machinery required for maturation of nuclear-encoded precursor proteins targeted to the mitochondrial matrix or inner membrane. We previously characterized this enzyme in rat (RMIP) and Saccharomyces cerevisiae (YMIP) and showed that MIP activity is essential for mitochondrial function in yeast. We have now defined the structure of a new MIP homologue ( SMIP) from the basidiomycete fungus Schizophyllum commune. SMIP includes 4 exons of 523, 486, 660, and 629 bp separated by 3 short introns. The predicted SMIP, YMIP, and RMIP sequences share 31-37% identity and 54-57% similarity over 700 amino acids. When SMIP and RMIP were expressed in a yeast mip1Δ mutant, they were both able to rescue the respiratory-deficient phenotype caused by genetic inactivation of YMIP, indicating that the function of this enzyme is conserved in eukaryotes. Moreover, the MIP sequences show 20-24% identity and 40-47% similarity to a family of oligopeptidases from bacteria, yeast, and mammals. MIP and these proteins are characterized by a highly conserved motif, F-H-E-X-G-H-(X) 2-H-(X) 12-G-(X) 5-D-(X) 2-E-X-P-S-(X) 3-E-X, centered around a zinc-binding site and appear to represent a new family of genes associated with proteolytic processing in the mitochondrial and cytosolic compartments.
Bibliography:	9559528 F30 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0888-7543 1089-8646
DOI:	10.1006/geno.1995.1174