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Tytuł pozycji:

Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif.

Tytuł :
Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif.
Autorzy :
Hendrick JP; Yale University School of Medicine, Department of Human Genetics, New Haven, CT 06510.
Hodges PE
Rosenberg LE
Pokaż więcej
Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1989 Jun; Vol. 86 (11), pp. 4056-60.
Typ publikacji :
Journal Article
Język :
English
Imprint Name(s) :
Original Publication: Washington, DC : National Academy of Sciences
MeSH Terms :
Enzyme Precursors/*genetics
Mitochondria/*enzymology
Peptide Hydrolases/*metabolism
Protein Sorting Signals/*genetics
Amino Acid Sequence ; Animals ; Humans ; Information Systems ; Molecular Sequence Data
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Molecular Sequence :
GENBANK J02622; J02634; J03190; J03548; J03621; K02064; K02100; M11266; M11746; M11770; M12105; M16229; M19680; X02156; X02472; X03517; X05218; X05219; Y00152; Y00451
Substance Nomenclature :
0 (Enzyme Precursors)
0 (Protein Sorting Signals)
EC 3.4.- (Peptide Hydrolases)
Entry Date(s) :
Date Created: 19890601 Date Completed: 19890712 Latest Revision: 20190501
Update Code :
20210623
PubMed Central ID :
PMC287387
DOI :
10.1073/pnas.86.11.4056
PMID :
2657736
Czasopismo naukowe
We have compiled sequences of precursor proteins for 50 mitochondrial proteins for which the mature amino terminus has been determined by amino acid sequence analysis. Included in this set are 8 precursors that have leader peptides that are cleaved in two places by mitochondrial matrix proteases. When these eight leader peptides are aligned and compared, a highly conserved three-amino acid motif is identified as being common to this class of leader peptides. This motif includes an arginine at position -10, a hydrophobic residue at position -8, and serine, threonine, or glycine at position -5 relative to the mature amino terminus. The initial cleavage of these peptides by matrix processing protease occurs within the motif, between residues at -9 and -8, such that arginine at position -10 is at position -2 relative to the cleaved bond. The rest of the motif is within the octapeptide removed by subsequent cleavage catalyzed by intermediate-specific protease. An additional 14 leader peptides in this collection (all of those that contain an arginine at -10) conform to this motif. Assuming that these 14 precursors are matured in two steps, we compared the internal cleavage sites at position -8 with the ends of the other 30 leader peptides in the collection. We find that 74% of matrix processing protease cleavage sites follow an arginine at position -2 relative to cleavage.

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