Plant Molecular Biology

, Volume 27, Issue 6, pp 1109–1118 | Cite as

Structure and expression of LeMA-1, a tomato protein belonging to the SEC18-PAS1-CDC48-TBP-1 protein family of putative Mg2+-dependent ATPases

  • Anastasia Prombona
  • Martin Tabler
  • Mary Providaki
  • Mina Tsagris
Research Article

Abstract

cDNA clones of a tomato protein, called Lycopersicum esculentum putative Mg2+-dependent ATPase (LeMA-1), were isolated from a cDNA library. Sequence comparison of the tomato protein with other genes in the database revealed that the protein is highly homologous to a human protein called TBP-1 and a yeast Tat-binding-analogue protein YTA1A. All three proteins belong to the recently discovered protein family of putative Mg2+-dependent ATPases and form within this family a subgroup of proteins involved in controlled protein degradation and possibly also in transcriptional regulation. Expression of the mRNA of LeMA-1 could be monitored in several plant tissues. LeMA-1 is the first member of this subgroup of proteins isolated from plants.

Key words

multicatalytic proteinase 26S protease proteasome seed germination 

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References

  1. 1.
    Altschul SF, Gish W, Miller W, Meyers EW, Lipman DJ: Basic local alignment research tool. J Mol Biol 215: 403–410 (1990).PubMedGoogle Scholar
  2. 2.
    Dubiel W, Ferrell K, Pratt G, Rechsteiner M: Subunit 4 of the 26S protease is a member of a novel eukaryotic ATPase family. J Biol Chem 267: 22699–22702 (1992).PubMedGoogle Scholar
  3. 3.
    Dubiel W, Ferrell K, Rechsteiner M: Peptide sequencing identifies MSS1, a modulator of HIV-Tat-mediated transactivation, as subunit 7 of the 26S protease. FEBS Lett 323: 276–278 (1993).CrossRefPubMedGoogle Scholar
  4. 4.
    Erdmann R, Wiebel FF, Flessau A, Rytka J, Beyer A, Frölich KU, Kunau WH: PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases. Cell 64: 499–510 (1991).CrossRefPubMedGoogle Scholar
  5. 5.
    Frölich K-U, Fries H-W, Rüdiger M, Erdmann R, Botstein D, Mecke D: Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation and gene expression. J Cell Biol 114: 443–453 (1990).CrossRefGoogle Scholar
  6. 6.
    Früh K, Gossen M, Wang K, Bujard H, Peterson PA, Yang Y: Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J 13: 3236–3244 (1994).PubMedGoogle Scholar
  7. 7.
    Genschik P, Jamet E, Philipps G, Parmentier Y, Gigot C, Fleck J: Molecular characterization of a β type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an α-type proteasome subunit early in the cell-cycle. Plant J 6: 537–546 (1994).CrossRefPubMedGoogle Scholar
  8. 8.
    Ghislain M, Udvardy A, Mann C: S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366: 358–362 (1993).CrossRefPubMedGoogle Scholar
  9. 9.
    Goldberg AL: The mechanisms and functions of ATP-dependent proteases in bacterial and animal cells. Eur J Biochem 203: 9–23 (1992).PubMedGoogle Scholar
  10. 10.
    Gordon C, McGurk G, Dillon P, Rosen C, Hastie ND: Defective mitosis due to a mutation in the gene for fission yeast 26S protease subunit. Nature 366: 355–357 (1993).CrossRefPubMedGoogle Scholar
  11. 11.
    Goyer C, Lee HS, Malo D, Sonenberg N: Isolation of a yeast gene encoding a protein homologous to the human Tat-binding protein TBP-1. DNA Cell Biol 11: 579–585 (1992).PubMedGoogle Scholar
  12. 12.
    Kozak M: Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem 266: 19867–19887 (1991).PubMedGoogle Scholar
  13. 13.
    Lütcke HA, Chow KC, Mickel FS, Moss KA, Kern HF, Scheele GA: Selection of AUG initiation codons differs in plants and animals. EMBO J 6: 43–48 (1987).PubMedGoogle Scholar
  14. 14.
    Lazarus CM: Gibberellin: coordinate and non coordinate gene expression. In: Grierson D (ed) Developmental Regulation of Plant Gene Expression, pp. 48–60. Blackie, Glasgow/London (1991).Google Scholar
  15. 15.
    Nelbock P, Dillon PJ, Perkins A, Rosen CA: A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. Science 248: 1650–1653 (1990).PubMedGoogle Scholar
  16. 16.
    Ohana B, Moore PA, Ruben SM, Southgate CD, Green MR, Rosen CA: The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes. Proc Natl Acad Sci USA 90: 138–142 (1993).PubMedGoogle Scholar
  17. 17.
    Peters J-M, Walsh MJ, Franke WW: An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J 9: 1757–1767 (1990).PubMedGoogle Scholar
  18. 18.
    Rechsteiner M, Hoffmann L, Dubiel W: Multicatalytic and 26S proteases. J Biol Chem 268: 6065–6068 (1993).PubMedGoogle Scholar
  19. 19.
    Rivett AJ: Proteasomes: multicatalytic proteinase complexes. Biochem J 291: 1–10 (1993).PubMedGoogle Scholar
  20. 20.
    Rivett AJ, Knecht E: Proteasome location. Curr Biol 3: 127–129 (1993).CrossRefPubMedGoogle Scholar
  21. 21.
    Saghai-Maroof MA, Solimann KM, Jorgensen RA, Allard RW: Ribosomal DNA spacer-length polymorphisms in barley: Mendelian inheritance, chromosomal location, and population dynamics. Proc Natl Acad Sci USA 81: 8014–8018 (1984).PubMedGoogle Scholar
  22. 22.
    Saira Mian I: Sequence similarities between cell regulation factors, heat shock proteins and RNA helicases. Trends Biochem Sci 37: 125–127 (1993).Google Scholar
  23. 23.
    Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).Google Scholar
  24. 24.
    Schnall R, Mannhaupt G, Stucka R, Tauer R, Ehnle S, Schwartzlose S, Vetter I, Feldmann H: Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10: 1141–1155 (1994).PubMedGoogle Scholar
  25. 25.
    Shanklin J, Jabben M, Viestra RD: Red light induced formation of ubiquitin-phytochrome conjugates. Proc Natl Acad Sci USA 84: 359–363 (1987).Google Scholar
  26. 26.
    Shaw DR, Enis HL: Molecular cloning and developmental regulation of Dictyostelium discoideum homologues of the human and yeast HIV1 Tat-binding protein. Biochem Biophys Res Comm 193: 1291–1296 (1993).CrossRefPubMedGoogle Scholar
  27. 27.
    Shibuya H, Irie K, Ninomiya-Tsuji J, Goebl M, Taniguchi T, Matsumoto K: New human gene encoding a positive modulator of HIV Tat-mediated transactivation. Nature 357: 700–702 (1992).CrossRefPubMedGoogle Scholar
  28. 28.
    Swaffield JC, Bromberg JF, Johnston SA: Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4. Nature 357: 698–700 (1992).CrossRefPubMedGoogle Scholar
  29. 29.
    Tabler M, Sänger HL: Infectivity studies on different potato spindle tuber viroid (PSTV) RNAs synthesized in vitro with the SP6 transcription system. EMBO J 4: 2191–2199 (1985).Google Scholar
  30. 30.
    Tabler M, Günther I, Kern R, Sänger HL: A microscale procedure for isolating and sequencing the viroid RNA present in one gram of infected leaf tissue. J Virol Meth 23: 111–126 (1989).CrossRefGoogle Scholar
  31. 31.
    Viestra RD: Protein degradation in plants. Annu Rev Plant Physiol Plant Mol Biol 44: 385–410 (1993).CrossRefGoogle Scholar
  32. 32.
    Vinson CR, LaMarco KL, Johnson PF, Landschulz WH, McKnight SL: In situ detection of sequence specific DNA binding activity specified by a recombinant bacteriophage. Genes Devel Dev 2: 801–806 (1988).Google Scholar

Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Anastasia Prombona
    • 1
  • Martin Tabler
    • 1
  • Mary Providaki
    • 1
  • Mina Tsagris
    • 1
  1. 1.Institute of Molecular Biology and BiotechnologyFoundation for Research and Technology — HellasHeraklionGreece

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