Biochemistry, Department of
Document Type
Article
Date of this Version
2008
Citation
MOLECULAR AND CELLULAR BIOLOGY, Aug. 2008, p. 4927–4939 Vol. 28, No. 16
Abstract
The assembly of cytochrome c oxidase (CcO) in yeast mitochondria is dependent on a new assembly factor designated Coa2. Coa2 was identified from its ability to suppress the respiratory deficiency of coa1 Δ and shy1 Δ cells. Coa1 and Shy1 function at an early step in maturation of the Cox1 subunit of CcO. Coa2 functions downstream of the Mss51-Coa1 step in Cox1 maturation and likely concurrent with the Shy1-related heme a3 insertion into Cox1. Coa2 interacts with Shy1. Cells lacking Coa2 show a rapid degradation of newly synthesized Cox1. Rapid Cox1 proteolysis also occurs in shy1 Δ cells, suggesting that in the absence of Coa2 or Shy1, Cox1 forms an unstable conformer. Overexpression of Cox10 or Cox5a and Cox6 or attenuation of the proteolytic activity of the m-AAA protease partially restores respiration in coa2 Δ cells. The matrix-localized Coa2 protein may aid in stabilizing an early Cox1 intermediate containing the nuclear subunits Cox5a and Cox6.
Included in
Biochemistry Commons, Biotechnology Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
Copyright © 2008, American Society for Microbiology. All Rights Reserved.