RGD Reference Report - Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteins. - Rat Genome Database

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Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteins.

Authors: Nagao, Y  Kitada, S  Kojima, K  Toh, H  Kuhara, S  Ogishima, T  Ito, A 
Citation: Nagao Y, etal., J Biol Chem. 2000 Nov 3;275(44):34552-6. doi: 10.1074/jbc.M003110200.
RGD ID: 38501073
Pubmed: PMID:10942759   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M003110200   (Journal Full-text)

Mitochondrial processing peptidase, a metalloendopeptidase consisting of alpha- and beta-subunits, specifically recognizes a large variety of mitochondrial precursor proteins and cleaves off amino-terminal extension peptides. The alpha-subunit has a characteristic glycine-rich segment in the middle portion. To elucidate the role of the region in processing functions of the enzyme, deletion or site-directed mutations were introduced, and effects on kinetic parameters and substrate binding of the enzyme were analyzed. Deletion of three residues of the region, Phe(289) to Ala(291), led to a dramatic reduction in processing activity to practically zero. Mutation of Phe(289), Lys(296), and Met(298) to alanine resulted in a decrease in the activity, but these mutations had no apparent effect on interactions between the two subunits, indicating that reduction in processing activity is not due to structural disruption at the interface interacting with the beta-subunit. Although the mutant enzymes, Phe289Ala, Lys296Ala, and Met298Ala, had an approximate 10-fold less affinity for substrate peptides than did that of the wild type, the deletion mutant, delta 289-291, showed an extremely low affinity. Thus, shortening of the glycine-rich stretch led to a dramatic reduction of interaction between the enzyme and substrate peptides and cleavage reaction, whereas mutation of each amino acid in this region seemed to affect primarily the cleavage reaction.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein processing involved_inIDA 38501073PMID:10942759UniProt 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
mitochondrial processing peptidase complex part_ofIDA 38501073PMID:10942759UniProt 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
metalloendopeptidase activity enablesIDA 38501073PMID:10942759UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Pmpcb  (peptidase, mitochondrial processing subunit beta)


Additional Information