Formation of molecular species of mitochondrial cardiolipin. 1. A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species

Biochim Biophys Acta. 2009 Apr;1791(4):314-20. doi: 10.1016/j.bbalip.2009.01.004. Epub 2009 Jan 21.


Mitochondrial cardiolipin undergoes extensive remodeling of its acyl groups to generate uniformly substituted species, such as tetralinoleoyl-cardiolipin, but the mechanism of this remodeling has not been elucidated, except for the fact that it requires tafazzin. Here we show that purified recombinant Drosophila tafazzin exchanges acyl groups between cardiolipin and phosphatidylcholine by a combination of forward and reverse transacylations. The acyl exchange is possible in the absence of phospholipase A(2) because it requires only trace amounts of lysophospholipids. We show that purified tafazzin reacts with various phospholipid classes and with various acyl groups both in sn-1 and sn-2 position. Expression studies in Sf9 insect cells suggest that the effect of tafazzin on cardiolipin species is dependent on the cellular environment and not on enzymatic substrate specificity. Our data demonstrate that tafazzin catalyzes general acyl exchange between phospholipids, which raises the question whether pattern formation in cardiolipin is the result of the equilibrium distribution of acyl groups between multiple phospholipid species.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • 1-Acylglycerophosphocholine O-Acyltransferase / metabolism
  • Acylation
  • Animals
  • Cardiolipins / metabolism*
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / metabolism*
  • Fatty Acids / metabolism*
  • Mitochondria, Liver / metabolism*
  • Phosphatidylcholines / metabolism*
  • Phospholipase A2 Inhibitors
  • Phospholipases A2 / metabolism
  • Rats


  • Cardiolipins
  • Drosophila Proteins
  • Fatty Acids
  • Phosphatidylcholines
  • Phospholipase A2 Inhibitors
  • 1-Acylglycerophosphocholine O-Acyltransferase
  • tafazzin protein, Drosophila
  • Phospholipases A2