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Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates.

Publication ,  Journal Article
Tan, BK; Bogdanov, M; Zhao, J; Dowhan, W; Raetz, CRH; Guan, Z
Published in: Proc Natl Acad Sci U S A
October 9, 2012

Depending on growth phase and culture conditions, cardiolipin (CL) makes up 5-15% of the phospholipids in Escherichia coli with the remainder being primarily phosphatidylethanolamine (PE) and phosphatidylglycerol (PG). In E. coli, the cls and ybhO genes (renamed clsA and clsB, respectively) each encode a CL synthase (Cls) that catalyzes the condensation of two PG molecules to form CL and glycerol. However, a ΔclsAB mutant still makes CL in the stationary phase, indicating the existence of additional Cls. We identified a third Cls encoded by ymdC (renamed clsC). ClsC has sequence homology with ClsA and ClsB, which all belong to the phospholipase D superfamily. The ΔclsABC mutant lacks detectible CL regardless of growth phase or growth conditions. CL can be restored to near wild-type levels in stationary phase in the triple mutant by expressing either clsA or clsB. Expression of clsC alone resulted in a low level of CL in the stationary phase, which increased to near wild-type levels by coexpression of its neighboring gene, ymdB. CL synthesis by all Cls is increased with increasing medium osmolarity during logarithmic growth and in stationary phase. However, only ClsA contributes detectible levels of CL at low osmolarity during logarithmic growth. Mutation of the putative catalytic motif of ClsC prevents CL formation. Unlike eukaryotic Cls (that use PG and CDP-diacylglycerol as substrates) or ClsA, the combined YmdB-ClsC used PE as the phosphatidyl donor to PG to form CL, which demonstrates a third and unique mode for CL synthesis.

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Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

October 9, 2012

Volume

109

Issue

41

Start / End Page

16504 / 16509

Location

United States

Related Subject Headings

  • Transferases (Other Substituted Phosphate Groups)
  • Tandem Mass Spectrometry
  • Substrate Specificity
  • Sequence Homology, Amino Acid
  • Phosphatidylglycerols
  • Phosphatidylethanolamines
  • Mutation
  • Molecular Sequence Data
  • Membrane Proteins
  • Isoenzymes
 

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Tan, B. K., Bogdanov, M., Zhao, J., Dowhan, W., Raetz, C. R. H., & Guan, Z. (2012). Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates. Proc Natl Acad Sci U S A, 109(41), 16504–16509. https://doi.org/10.1073/pnas.1212797109
Tan, Brandon K., Mikhail Bogdanov, Jinshi Zhao, William Dowhan, Christian R. H. Raetz, and Ziqiang Guan. “Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates.Proc Natl Acad Sci U S A 109, no. 41 (October 9, 2012): 16504–9. https://doi.org/10.1073/pnas.1212797109.
Tan BK, Bogdanov M, Zhao J, Dowhan W, Raetz CRH, Guan Z. Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16504–9.
Tan, Brandon K., et al. “Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates.Proc Natl Acad Sci U S A, vol. 109, no. 41, Oct. 2012, pp. 16504–09. Pubmed, doi:10.1073/pnas.1212797109.
Tan BK, Bogdanov M, Zhao J, Dowhan W, Raetz CRH, Guan Z. Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates. Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16504–16509.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

October 9, 2012

Volume

109

Issue

41

Start / End Page

16504 / 16509

Location

United States

Related Subject Headings

  • Transferases (Other Substituted Phosphate Groups)
  • Tandem Mass Spectrometry
  • Substrate Specificity
  • Sequence Homology, Amino Acid
  • Phosphatidylglycerols
  • Phosphatidylethanolamines
  • Mutation
  • Molecular Sequence Data
  • Membrane Proteins
  • Isoenzymes