PMID- 21476578
OWN - NLM
STAT- MEDLINE
DCOM- 20110801
LR  - 20211020
IS  - 1520-4995 (Electronic)
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 50
IP  - 19
DP  - 2011 May 17
TI  - Cardiolipin deficiency in Rhodobacter sphaeroides alters the lipid profile of 
      membranes and of crystallized cytochrome oxidase, but structure and function are 
      maintained.
PG  - 3879-90
LID - 10.1021/bi101702c [doi]
AB  - Many recent studies highlight the importance of lipids in membrane proteins, 
      including in the formation of well-ordered crystals. To examine the effect of 
      changes in one lipid, cardiolipin, on the lipid profile and the production, 
      function, and crystallization of an intrinsic membrane protein, cytochrome c 
      oxidase, we mutated the cardiolipin synthase (cls) gene of Rhodobacter 
      sphaeroides, causing a >90% reduction in cardiolipin content in vivo and 
      selective changes in the abundances of other lipids. Under these conditions, a 
      fully native cytochrome c oxidase (CcO) was produced, as indicated by its 
      activity, spectral properties, and crystal characteristics. Analysis by MALDI 
      tandem mass spectrometry (MS/MS) revealed that the cardiolipin level in CcO 
      crystals, as in the membranes, was greatly decreased. Lipid species present in 
      the crystals were directly analyzed for the first time using MS/MS, documenting 
      their identities and fatty acid chain composition. The fatty acid content of 
      cardiolipin in R. sphaeroides CcO (predominantly 18:1) differs from that in 
      mammalian CcO (18:2). In contrast to the cardiolipin dependence of mammalian CcO 
      activity, major depletion of cardiolipin in R. sphaeroides did not impact any 
      aspect of CcO structure or behavior, suggesting a greater tolerance of 
      interchange of cardiolipin with other lipids in this bacterial system.
FAU - Zhang, Xi
AU  - Zhang X
AD  - Department of Biochemistry and Molecular Biology, Michigan State University, East 
      Lansing, Michigan 48824, United States.
FAU - Tamot, Banita
AU  - Tamot B
FAU - Hiser, Carrie
AU  - Hiser C
FAU - Reid, Gavin E
AU  - Reid GE
FAU - Benning, Christoph
AU  - Benning C
FAU - Ferguson-Miller, Shelagh
AU  - Ferguson-Miller S
LA  - eng
GR  - R01 GM026916/GM/NIGMS NIH HHS/United States
GR  - R37 GM026916/GM/NIGMS NIH HHS/United States
GR  - R37 GM026916-31/GM/NIGMS NIH HHS/United States
GR  - R01 GM26916/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20110422
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Cardiolipins)
RN  - 0 (Membrane Lipids)
RN  - 0 (Membrane Proteins)
RN  - EC 1.9.3.1 (Electron Transport Complex IV)
RN  - EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups))
RN  - EC 2.7.8.- (cardiolipin synthetase)
SB  - IM
MH  - *Cardiolipins/biosynthesis/chemistry/metabolism
MH  - Crystallization
MH  - Electron Transport Complex IV/biosynthesis/*chemistry/genetics
MH  - Gene Deletion
MH  - Gene Expression Regulation, Bacterial/genetics
MH  - *Lipid Metabolism/physiology
MH  - Membrane Lipids/biosynthesis/*chemistry/*deficiency
MH  - Membrane Proteins/deficiency/genetics
MH  - Rhodobacter sphaeroides/*enzymology/genetics/growth & development
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Structure-Activity Relationship
MH  - Tandem Mass Spectrometry
MH  - Transferases (Other Substituted Phosphate Groups)/deficiency/genetics
PMC - PMC3097902
MID - NIHMS291508
EDAT- 2011/04/12 06:00
MHDA- 2011/08/02 06:00
PMCR- 2012/05/17
CRDT- 2011/04/12 06:00
PHST- 2011/04/12 06:00 [entrez]
PHST- 2011/04/12 06:00 [pubmed]
PHST- 2011/08/02 06:00 [medline]
PHST- 2012/05/17 00:00 [pmc-release]
AID - 10.1021/bi101702c [doi]
PST - ppublish
SO  - Biochemistry. 2011 May 17;50(19):3879-90. doi: 10.1021/bi101702c. Epub 2011 Apr 
      22.