Theses and Dissertations
Issuing Body
Mississippi State University
Advisor
Gordon, Donna M.
Committee Member
Kavazis, Andreas N.
Committee Member
Stewart, James A., Jr.
Date of Degree
12-14-2013
Original embargo terms
MSU Only Indefinitely
Document Type
Graduate Thesis - Campus Access Only
Major
Biological Sciences
Degree Name
Master of Science
College
College of Arts and Sciences
Department
Department of Biological Sciences
Abstract
The rhomboid protease, Pcp1p, localizes to the mitochondrial inner membrane in Saccharomyces cerevisiae. The 346 amino acid protein contains an N-terminal mitochondria targeting signal followed by 6 transmembrane helices. Pcp1p substrates include, Ccp1p and Mgm1p; both soluble intermembrane space proteins after Pcp1p cleavage. Haploid pcp1 mutants grow slow, lose mitochondrial DNA, and have abnormal mitochondrial morphology; phenotypes similar to mgm1 mutants. Processing of Mgm1p depends on Pcp1p activity, matrix ATP levels, and a functional Tim23-Pam complex. This suggests a potential link between Pcp1p and the Tim23 complex. To test this hypothesis, epitope tagged versions of Pcp1p, Tim23p, Tim21p, and Pam18p were generated for use in immunoprecipitation and sucrose gradient ultracentrifugation experiments. The data suggest that Pcp1p exists in a higher order protein complex that may contain multiple Pcp1p subunits and components of the Tim23 translocon. The importance of this interaction in the processing of precursor proteins remains to be determined.
URI
https://hdl.handle.net/11668/19050
Recommended Citation
Othan, Adef, "Biochemical Characterization of the Saccharomyces Cerevisiae Mitochondrial Rhomboid Protease, Pcp1p" (2013). Theses and Dissertations. 877.
https://scholarsjunction.msstate.edu/td/877