NDLI: Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP).

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Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP).

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Timing and structural consideration for the processing of mitochondrial matrix space proteins by the mitochondrial processing peptidase (MPP).

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mukhopadhyay, Abhijit Hammen, Philip Waltner-Law, Mary Weiner, Henry
Description	Country affiliation: United States Author Affiliation: Mukhopadhyay A ( Department of Biochemistry, Purdue University, West Lafayette, IN 47907-1153, USA.)
Abstract	Most mitochondrial matrix space proteins are synthesized as a precursor protein, and the N-terminal extension of amino acids that served as the leader sequence is removed after import by the action of a metalloprotease called mitochondrial processing peptidase (MPP). The crystal structure of MPP has been solved very recently, and it has been shown that synthetic leader peptides bind with MPP in an extended conformation. However, it is not known how MPP recognizes hundreds of leader peptides with different primary and secondary structures or when during import the leader is removed. Here we took advantage of the fact that the structure of the leader from rat liver aldehyde dehydrogenase has been determined by 2D-NMR to possess two helical portions separated by a three amino acid (RGP) linker. When the linker was deleted, the leader formed one long continuous helix that can target a protein to the matrix space but is not removed by the action of MPP. Repeats of two and three leaders were fused to the precursor protein to determine the stage of import at which processing occurs, if MPP could function as an endo peptidase, and if it would process if the cleavage site was part of a helix. Native or linker deleted constructs were used. Import into isolated yeast mitochondria or processing with recombinantly expressed MPP was performed. It was concluded that processing did not occur as the precursor was just entering the matrix space, but most likely coincided with the folding of the protein. Further, finding that hydrolysis could not take place if the processing site was part of a stable helix is consistent with the crystal structure of MPP. Lastly, it was found that MPP could function at sites as far as 108 residues from the N terminus of the precursor protein, but its ability to process decreases exponentially as the distance increases.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	11
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2002-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Metalloendopeptidases Metabolism Mitochondrial Proteins Protein Processing, Post-translational Aldehyde Dehydrogenase Amino Acid Sequence Escherichia Coli Molecular Sequence Data Protein Sorting Signals Recombinant Fusion Proteins Saccharomyces Cerevisiae Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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