Identification of the Matrix Targeting and Stop Transfer Domains in the Presequence of the Mitochondrial Intermembrane Space Protein Cytochrome C Peroxidase

The presequence of CCP, an intermembrane space heme protein, has been proposed to be composed of an amino-terminal basic domain, a stretch of hydrophobic residues and a basic, carboxy-terminal domain (Kaput et al, 1982). Results from previous in vitro import experiments with a mutant ccp that was missing ten alanines from its hydrophobic domain implied that this mutant was targeted to the mitochondrial matrix (Ekberg and Kaput, in preparation). This study utilized an in vivo approach to confirm the results obtained from analyzing import into isolated mitochondria and supporting the suggestion that the hydrophobic domain acts as a stop transfer sequence.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2014

Author dc:creator

• Kirchner, Sandra Chapman

Contributors dc:contributor

• Kaput, James,

• Biology, Molecular

Identifier

(UMI)AAI9305582

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/72352