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Purified inner membrane protease I of yeast mitochondria is a heterodimer

Schneider, A. and Oppliger, W. and Jeno, P.. (1994) Purified inner membrane protease I of yeast mitochondria is a heterodimer. Journal of biological chemistry, Vol. 269 , no. 12. pp. 8635-8638.

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Official URL: http://edoc.unibas.ch/dok/A5258324

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Abstract

Inner membrane protease I is bound to the outer face of the yeast mitochondrial inner membrane and mediates the proteolytic maturation of cytochrome b2 and cytochrome oxidase subunit II. We have previously shown that one of its subunits is a 21.4-kDa integral membrane protein encoded by the nuclear IMP1 gene. We have now purified the active protease approximately 300-fold from yeast mitochondria. It has an apparent molecular weight of 35,000 and contains not only Imp1p but also a previously unrecognized 19-kDa subunit. Partial amino acid sequencing identifies this subunit as the product of the recently described IMP2 gene (Nunnari, J., Fox, T., and Walter, P. (1993) Science 262, 1997-2004).
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > Mass Spectrometry (Jenö)
UniBasel Contributors:Jenö, Paul
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Society of Biological Chemists
ISSN:0021-9258
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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