PMID- 19841065
OWN - NLM
STAT- MEDLINE
DCOM- 20100114
LR  - 20220224
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 30
IP  - 1
DP  - 2010 Jan
TI  - The role of Coa2 in hemylation of yeast Cox1 revealed by its genetic interaction 
      with Cox10.
PG  - 172-85
LID - 10.1128/MCB.00869-09 [doi]
AB  - Saccharomyces cerevisiae cells lacking the cytochrome c oxidase (CcO) assembly 
      factor Coa2 are impaired in Cox1 maturation and exhibit a rapid degradation of 
      newly synthesized Cox1. The respiratory deficiency of coa2 Delta cells is 
      suppressed either by the presence of a mutant allele of the Cox10 farnesyl 
      transferase involved in heme a biosynthesis or through impaired proteolysis by 
      the disruption of the mitochondrial Oma1 protease. Cox10 with an N196K 
      substitution functions as a robust gain-of-function suppressor of the respiratory 
      deficiency of coa2 Delta cells but lacks suppressor activity for two other CcO 
      assembly mutant strains, the coa1 Delta and shy1 Delta mutants. The suppressor 
      activity of N196K mutant Cox10 is dependent on its catalytic function and the 
      presence of Cox15, the second enzyme involved in heme a biosynthesis. Varying the 
      substitution at Asn196 reveals a correlation between the suppressor activity and 
      the stabilization of the high-mass homo-oligomeric Cox10 complex. We postulate 
      that the mutant Cox10 complex has enhanced efficiency in the addition of heme a 
      to Cox1. Coa2 appears to impart stability to the oligomeric wild-type Cox10 
      complex involved in Cox1 hemylation.
FAU - Bestwick, Megan
AU  - Bestwick M
AD  - University of Utah Health Sciences Center, Department of Medicine, Salt Lake 
      City, UT 84132, USA.
FAU - Khalimonchuk, Oleh
AU  - Khalimonchuk O
FAU - Pierrel, Fabien
AU  - Pierrel F
FAU - Winge, Dennis R
AU  - Winge DR
LA  - eng
GR  - R01 ES003817/ES/NIEHS NIH HHS/United States
GR  - R37 ES003817/ES/NIEHS NIH HHS/United States
GR  - T32 DK007115/DK/NIDDK NIH HHS/United States
GR  - ES03817/ES/NIEHS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Coa2 protein, S cerevisiae)
RN  - 0 (Membrane Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 18535-39-2 (heme a)
RN  - 42VZT0U6YR (Heme)
RN  - EC 1.9.3.1 (Cox1 protein, S cerevisiae)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 2.5.- (Alkyl and Aryl Transferases)
RN  - EC 2.5.1.- (COX10 protein, S cerevisiae)
RN  - EC 3.4.- (Metalloproteases)
RN  - EC 3.4.- (Oma1 protein, S cerevisiae)
SB  - IM
MH  - Alkyl and Aryl Transferases/genetics/*metabolism
MH  - Catalysis
MH  - Electron Transport Complex IV/genetics/*metabolism
MH  - Heme/*analogs & derivatives/metabolism
MH  - Membrane Proteins/genetics/*metabolism/*physiology
MH  - Metalloproteases/genetics/metabolism
MH  - Mutation
MH  - Saccharomyces cerevisiae/*metabolism
MH  - Saccharomyces cerevisiae Proteins/genetics/*metabolism/*physiology
PMC - PMC2798283
EDAT- 2009/10/21 06:00
MHDA- 2010/01/15 06:00
PMCR- 2010/07/01
CRDT- 2009/10/21 06:00
PHST- 2009/10/21 06:00 [entrez]
PHST- 2009/10/21 06:00 [pubmed]
PHST- 2010/01/15 06:00 [medline]
PHST- 2010/07/01 00:00 [pmc-release]
AID - MCB.00869-09 [pii]
AID - 0869-09 [pii]
AID - 10.1128/MCB.00869-09 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2010 Jan;30(1):172-85. doi: 10.1128/MCB.00869-09.