Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Author(s): Aygun-Sunar S;Aygun-Sunar S; Bilaloglu R; Goldfine H; Daldal F
  • Source:
    Journal of bacteriology [J Bacteriol] 2007 Dec; Vol. 189 (23), pp. 8564-74. Date of Electronic Publication: 2007 Oct 05.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5530 (Electronic) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : American Society for Microbiology
    • Subject Terms:
      1-Acylglycerol-3-Phosphate O-Acyltransferase/*genetics ; Glycerol-3-Phosphate O-Acyltransferase/*genetics ; Lipids/*biosynthesis ; Ornithine/*analogs & derivatives ; Phosphatidic Acids/*biosynthesis ; Rhodobacter capsulatus/*enzymology; 1-Acylglycerol-3-Phosphate O-Acyltransferase/metabolism ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cytochromes c/genetics ; Cytochromes c/metabolism ; Gene Expression Regulation, Bacterial ; Glycerol-3-Phosphate O-Acyltransferase/metabolism ; Glycerophospholipids/metabolism ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Ornithine/biosynthesis
    • Abstract:
      The Rhodobacter capsulatus genome contains three genes (olsA [plsC138], plsC316, and plsC3498) that are annotated as lysophosphatidic acid (1-acyl-sn-glycerol-3-phosphate) acyltransferase (AGPAT). Of these genes, olsA was previously shown to be an O-acyltransferase in the second step of ornithine lipid biosynthesis, which is important for optimal steady-state levels of c-type cytochromes (S. Aygun-Sunar, S. Mandaci, H.-G. Koch, I. V. J. Murray, H. Goldfine, and F. Daldal. Mol. Microbiol. 61:418-435, 2006). The roles of the remaining plsC316 and plsC3498 genes remained unknown. In this work, these genes were cloned, and chromosomal insertion-deletion mutations inactivating them were obtained to define their function. Characterization of these mutants indicated that, unlike the Escherichia coli plsC, neither plsC316 nor plsC3498 was essential in R. capsulatus. In contrast, no plsC316 olsA double mutant could be isolated, indicating that an intact copy of either olsA or plsC316 was required for R. capsulatus growth under the conditions tested. Compared to OlsA null mutants, PlsC316 null mutants contained ornithine lipid and had no c-type cytochrome-related phenotype. However, they exhibited slight growth impairment and highly altered total fatty acid and phospholipid profiles. Heterologous expression in an E. coli plsC(Ts) mutant of either R. capsulatus plsC316 or olsA gene products supported growth at a nonpermissive temperature, exhibited AGPAT activity in vitro, and restored phosphatidic acid biosynthesis. The more vigorous AGPAT activity displayed by PlsC316 suggested that plsC316 encodes the main AGPAT required for glycerophospholipid synthesis in R. capsulatus, while olsA acts as an alternative AGPAT that is specific for ornithine lipid synthesis. This study therefore revealed for the first time that some OlsA enzymes, like the enzyme of R. capsulatus, are bifunctional and involved in both membrane ornithine lipid and glycerophospholipid biosynthesis.
    • References:
      Mol Microbiol. 2006 Jul;61(2):418-35. (PMID: 16856942)
      Plant Cell. 2005 Apr;17(4):1073-89. (PMID: 15772283)
      J Mol Biol. 1979 Jun 25;131(2):157-68. (PMID: 490646)
      J Bacteriol. 1997 Nov;179(22):6921-8. (PMID: 9371435)
      J Biol Chem. 1993 Oct 15;268(29):22156-63. (PMID: 8408076)
      J Bacteriol. 1997 Dec;179(23):7257-63. (PMID: 9393688)
      J Biol Chem. 1998 Feb 13;273(7):4096-105. (PMID: 9461603)
      Plant Mol Biol. 1994 Oct;26(1):211-23. (PMID: 7948871)
      J Biol Chem. 1975 Nov 10;250(21):8530-5. (PMID: 387)
      DNA Cell Biol. 1997 Jun;16(6):691-701. (PMID: 9212163)
      J Biol Chem. 1981 Jan 25;256(2):736-42. (PMID: 7005223)
      Nature. 1970 Aug 15;227(5259):680-5. (PMID: 5432063)
      Mol Microbiol. 1995 Nov;18(3):401-12. (PMID: 8748025)
      Mol Microbiol. 1999 Jun;32(5):942-52. (PMID: 10361297)
      Biochem J. 1997 Sep 1;326 ( Pt 2):455-61. (PMID: 9291118)
      J Biol Chem. 1997 Aug 8;272(32):20299-305. (PMID: 9242711)
      J Biol Chem. 1982 Sep 25;257(18):10759-65. (PMID: 6809756)
      Expert Opin Ther Targets. 2003 Oct;7(5):643-61. (PMID: 14498826)
      Plant Physiol. 1995 Nov;109(3):999-1006. (PMID: 8552723)
      FEMS Microbiol Lett. 1994 May 15;118(3):227-31. (PMID: 8020746)
      Proc Natl Acad Sci U S A. 1980 Dec;77(12):7347-51. (PMID: 7012838)
      Mol Gen Genet. 1992 Mar;232(2):295-303. (PMID: 1557036)
      Microbiology (Reading). 2005 Sep;151(Pt 9):3071-3080. (PMID: 16151217)
      J Biol Chem. 1990 Oct 5;265(28):17215-21. (PMID: 2211622)
      J Bacteriol. 1998 Mar;180(6):1425-30. (PMID: 9515909)
      Eur J Biochem. 1999 Nov;266(1):1-16. (PMID: 10542045)
      J Histochem Cytochem. 1982 Oct;30(10):1079-82. (PMID: 6182185)
      Biochem J. 2005 Jan 15;385(Pt 2):469-77. (PMID: 15367102)
      Plant Mol Biol. 1995 Oct;29(2):267-78. (PMID: 7579178)
      J Biol Chem. 1991 Nov 5;266(31):20732-43. (PMID: 1657935)
      Proc Natl Acad Sci U S A. 1986 Apr;83(7):2012-6. (PMID: 16593675)
      J Hum Genet. 2003;48(8):438-442. (PMID: 12938015)
      Anal Biochem. 1976 Sep;75(1):168-76. (PMID: 822747)
      Mol Cell. 2006 Sep 1;23(5):765-72. (PMID: 16949372)
      J Gen Microbiol. 1960 Jun;22:778-85. (PMID: 14447230)
      J Bacteriol. 1998 Feb;180(4):969-78. (PMID: 9473054)
      Prog Lipid Res. 1999 Sep-Nov;38(5-6):461-79. (PMID: 10793891)
      Microbiology (Reading). 2005 Aug;151(Pt 8):2529-2542. (PMID: 16079332)
      Plasmid. 1985 Mar;13(2):149-53. (PMID: 2987994)
      Plant Physiol. 1999 Jul;120(3):913-22. (PMID: 10398728)
      Eur J Biochem. 1995 Sep 15;232(3):806-10. (PMID: 7588719)
      DNA Seq. 2005 Oct;16(5):386-90. (PMID: 16243729)
      Biochem Biophys Res Commun. 1997 Aug 28;237(3):663-6. (PMID: 9299423)
      Mol Microbiol. 2002 Aug;45(3):721-33. (PMID: 12139618)
      Anal Biochem. 1987 Nov 1;166(2):368-79. (PMID: 2449095)
      J Bacteriol. 1997 Apr;179(8):2623-31. (PMID: 9098061)
    • Grant Information:
      R01 AI045153 United States AI NIAID NIH HHS; R01 GM038237 United States GM NIGMS NIH HHS; GM38237 United States GM NIGMS NIH HHS; AI45153 United States AI NIAID NIH HHS
    • Accession Number:
      0 (Bacterial Proteins)
      0 (Glycerophospholipids)
      0 (Lipids)
      0 (Phosphatidic Acids)
      0 (ornithine containing aminolipid)
      9007-43-6 (Cytochromes c)
      E524N2IXA3 (Ornithine)
      EC 2.3.1.15 (Glycerol-3-Phosphate O-Acyltransferase)
      EC 2.3.1.51 (1-Acylglycerol-3-Phosphate O-Acyltransferase)
    • Publication Date:
      Date Created: 20071009 Date Completed: 20071227 Latest Revision: 20211020
    • Publication Date:
      20221213
    • Accession Number:
      PMC2168953
    • Accession Number:
      10.1128/JB.01121-07
    • Accession Number:
      17921310