Skip to main content
SpringerLink
Log in

Characterization of Zea mays endosperm C-24 sterol methyltransferase: one of two types of sterol methyltransferase in higher plants

  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

We report the characterization of a higher-plant C-24 sterol methyltransferase by yeast complementation. A Zea mays endosperm expressed sequence tag (EST) was identified which, upon complete sequencing, showed 46% identity to the yeast C-24 methyltransferase gene (ERG6) and 75% and 37% amino acid identity to recently isolated higher-plant sterol methyltransferases from soybean and Arabidopsis, respectively. When placed under GAL4 regulation, the Z. mays cDNA functionally complemented the erg6 mutation, restoring ergosterol production and conferring resistance to cycloheximide. Complementation was both plasmid-dependent and galactose-inducible. The Z. mays cDNA clone contains an open reading frame encoding a 40 kDa protein containing motifs common to a large number of S-adenosyl-L-methionine methyltransferases (SMTs). Sequence comparisons and functional studies of the maize, soybean and Arabidopsis cDNAs indicates two types of C-24 SMTs exist in higher plants.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Becker MD, Guarente L: High efficiency transformation of yeast by electroporation. Meth Enzymol 194: 182-187 (1991).

    PubMed  Google Scholar 

  2. Benveniste P: Sterol biosynthesis. Annu Rev Plant Physiol 37: 275-308 (1986).

    Google Scholar 

  3. Chappell J, Wolf F, Prouix J, Cueller R, Saunders C: Is the reaction catalyzed by 3-hydroxy-3-methylglutaryl coenzyme A reductase a rate limiting step for isoprenoid biosynthesis in plants? Plant Physiol 109: 1337-1343 (1995).

    PubMed  Google Scholar 

  4. d'Enfert C, Minet M, Lacroute F: Cloning plant genes by complementation of yeastmutants. Meth Plant Cell Biol 49 (part B): 417-429 (1995).

    Google Scholar 

  5. Elledge SJ, Mulligan JT, Ramer SW, Spottswood M, Davis RW: λYES:Amultifunctional cDNAexpression vector for isolation of genes by complementation of yeast and Escherichia colimutations. Proc Natl Acad Sci USA 88: 1731-1735 (1991).

    PubMed  Google Scholar 

  6. Garber RF, Copple DM, Kennedy BK, Vidal M, Bard M: The yeast gene ERG6is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol Cell Biol 9: 3447-3456 (1989).

    PubMed  Google Scholar 

  7. Hoffman CS, Winston F: A ten minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57: 267-272 (1987).

    Article  PubMed  Google Scholar 

  8. Husselstein T, Gachotte D, Desprez T, Bard M, Benveniste P: Transformation of Saccharomyces cerevisiaewith a cDNA encoding a sterol C-methyltransferase from Arabidopsis thalianaresults in the synthesis of 24-ethyl sterols. FEBS Lett 381: 87-92 (1996).

    Article  PubMed  Google Scholar 

  9. Kagen RM, Clarke S: Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys 310: 417-427 (1994).

    Article  PubMed  Google Scholar 

  10. Moore JT, Gaylor JL: Isolation and purification of an Sadenosylmethionine: Δ24-sterolmethyltransferase fromyeast. J Biol Chem 244: 6334-6340 (1969).

    PubMed  Google Scholar 

  11. Nes WD, Janssen GG, Bergenstrahle A: Structural requirements for transformation of substrates by the (S)-adenosyl-Lmethionine: Δ24(25)-sterol methyl transferase. J Biol Chem 266: 15202-15212 (1991).

    PubMed  Google Scholar 

  12. Rahier A, Benveniste P: Mass spectral identification of phytosterols. In: New WD, Parish EJ (eds) Analysis of Sterol and Other Biologically Significant Steroids, pp. 223-250. Academic Press Publishers, New York (1989).

    Google Scholar 

  13. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual. Cold Springs Harbor Laboratory Press, Cold Spring Harbor, NY (1989).

    Google Scholar 

  14. Shi J, Gonzales RA, Bhattacharyya M: Identification and characterization of an S-adenosyl-L-methionine: Δ24-sterol-C-methyltransferase cDNA from soybean. J Biol Chem 271: 9384-9387 (1996).

    Article  PubMed  Google Scholar 

Download references

Author information

Author notes

  1. Robert J. Grebenok

    Present address: Department of Biology, Canisius College, Buffalo, NY, 14208, USA

Authors and Affiliations

  1. Department of Plant Sciences, University of Arizona, Tucson, AZ, 85721, USA

    Robert J. Grebenok & David W. Galbraith

  2. Department of Biochemistry, University of Nevada-Reno, Reno, NV, 89557, USA

    Dean Della Penna

Authors
  1. Robert J. Grebenok
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. David W. Galbraith
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Dean Della Penna
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Grebenok, R.J., Galbraith, D.W. & Della Penna, D. Characterization of Zea mays endosperm C-24 sterol methyltransferase: one of two types of sterol methyltransferase in higher plants. Plant Mol Biol 34, 891–896 (1997). https://doi.org/10.1023/A:1005818210641

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1005818210641

Search

Navigation