PMID- 22669974
OWN - NLM
STAT- MEDLINE
DCOM- 20121105
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 287
IP  - 32
DP  - 2012 Aug 3
TI  - Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated 
      by cytochrome oxidase assembly factor Coa2.
PG  - 26715-26
LID - 10.1074/jbc.M112.377200 [doi]
AB  - The synthesis of the heme a cofactor used in cytochrome c oxidase (CcO) is 
      dependent on the sequential action of heme o synthase (Cox10) and heme a synthase 
      (Cox15). The active state of Cox10 appears to be a homo-oligomeric complex, and 
      formation of this complex is dependent on the newly synthesized CcO subunit Cox1 
      and the presence of an early Cox1 assembly intermediate. Cox10 multimerization is 
      triggered by progression of Cox1 from the early assembly intermediate to 
      downstream intermediates. The CcO assembly factor Coa2 appears important in 
      coupling the presence of newly synthesized Cox1 to Cox10 oligomerization. Cells 
      lacking Coa2 are impaired in Cox10 complex formation as well as the formation of 
      a high mass Cox15 complex. Increasing Cox1 synthesis in coa2Delta cells restores 
      respiratory function if Cox10 protein levels are elevated. The C-terminal segment 
      of Cox1 is important in triggering Cox10 oligomerization. Expression of the 
      C-terminal 54 residues of Cox1 appended to a heterologous matrix protein leads to 
      efficient Cox10 complex formation in coa2Delta cells, but it fails to induce Cox15 
      complex formation. The state of Cox10 was evaluated in mutants, which predispose 
      human patients to CcO deficiency and the neurological disorder Leigh syndrome. 
      The presence of the D336V mutation in the yeast Cox10 backbone results in a 
      catalytically inactive enzyme that is fully competent to oligomerize. Thus, Cox10 
      oligomerization and catalytic activation are separate processes and can be 
      uncoupled.
FAU - Khalimonchuk, Oleh
AU  - Khalimonchuk O
AD  - Department of Medicine, University of Utah Health Sciences Center, Salt Lake 
      City, Utah 84132, USA.
FAU - Kim, Hyung
AU  - Kim H
FAU - Watts, Talina
AU  - Watts T
FAU - Perez-Martinez, Xochitl
AU  - Perez-Martinez X
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
DEP - 20120605
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Biopolymers)
RN  - 0 (Coa2 protein, S cerevisiae)
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
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)
SB  - IM
MH  - Alkyl and Aryl Transferases/*metabolism
MH  - Base Sequence
MH  - Biopolymers/*metabolism
MH  - DNA Primers
MH  - Electron Transport Complex IV/biosynthesis/*metabolism
MH  - Membrane Proteins/*metabolism
MH  - Saccharomyces cerevisiae/enzymology/metabolism
MH  - Saccharomyces cerevisiae Proteins/*metabolism
PMC - PMC3411010
EDAT- 2012/06/07 06:00
MHDA- 2012/11/06 06:00
PMCR- 2013/08/03
CRDT- 2012/06/07 06:00
PHST- 2012/06/07 06:00 [entrez]
PHST- 2012/06/07 06:00 [pubmed]
PHST- 2012/11/06 06:00 [medline]
PHST- 2013/08/03 00:00 [pmc-release]
AID - S0021-9258(20)47866-4 [pii]
AID - M112.377200 [pii]
AID - 10.1074/jbc.M112.377200 [doi]
PST - ppublish
SO  - J Biol Chem. 2012 Aug 3;287(32):26715-26. doi: 10.1074/jbc.M112.377200. Epub 2012 
      Jun 5.