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. 1994 Mar;6(3):351–360. doi: 10.1105/tpc.6.3.351

The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals.

A Goday 1, A B Jensen 1, F A Culiáñez-Macià 1, M Mar Albà 1, M Figueras 1, J Serratosa 1, M Torrent 1, M Pagès 1
PMCID: PMC160438  PMID: 8180497

Abstract

The maize abscisic acid (ABA)-responsive rab17 mRNA and Rab17 protein distribution in maize embryo tissues was investigated by in situ hybridization and immunocytochemistry. rab17 mRNA and Rab17 protein were found in all cells of embryo tissues. Synthesis of rab17 mRNA occurred initially in the embryo axis. As maturation progressed, rab17 mRNA was detectable in the scutellum and accumulated in axis cells and provascular tissues. However, the response to exogenous ABA differed in various embryo cell types. The Rab17 protein was located in the nucleus and in the cytoplasm, and qualitative differences in the phosphorylation states of the protein were found between the two subcellular compartments. Based on the similar domain arrangements of Rab17 and a nuclear localization signal (NLS) binding phosphoprotein, Nopp140, interaction of Rab17 with NLS peptides was studied. We found specific binding of Rab17 to the wild-type NLS of the SV40 T antigen but not to an import incompetent mutant peptide. Moreover, binding of the NLS peptide to Rab17 was found to be dependent upon phosphorylation. These results suggest that Rab17 may play a role in nuclear protein transport.

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Selected References

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  1. Adam S. A., Lobl T. J., Mitchell M. A., Gerace L. Identification of specific binding proteins for a nuclear location sequence. Nature. 1989 Jan 19;337(6204):276–279. doi: 10.1038/337276a0. [DOI] [PubMed] [Google Scholar]
  2. Albericio F., Andreu D., Giralt E., Navalpotro C., Pedroso E., Ponsati B., Ruiz-Gayo M. Use of the Npys thiol protection in solid phase peptide synthesis. Application to direct peptide-protein conjugation through cysteine residues. Int J Pept Protein Res. 1989 Aug;34(2):124–128. doi: 10.1111/j.1399-3011.1989.tb01500.x. [DOI] [PubMed] [Google Scholar]
  3. Coen E. S., Romero J. M., Doyle S., Elliott R., Murphy G., Carpenter R. floricaula: a homeotic gene required for flower development in antirrhinum majus. Cell. 1990 Dec 21;63(6):1311–1322. doi: 10.1016/0092-8674(90)90426-f. [DOI] [PubMed] [Google Scholar]
  4. Dure L., 3rd A repeating 11-mer amino acid motif and plant desiccation. Plant J. 1993 Mar;3(3):363–369. doi: 10.1046/j.1365-313x.1993.t01-19-00999.x. [DOI] [PubMed] [Google Scholar]
  5. Forbes D. J. Structure and function of the nuclear pore complex. Annu Rev Cell Biol. 1992;8:495–527. doi: 10.1146/annurev.cb.08.110192.002431. [DOI] [PubMed] [Google Scholar]
  6. Garcia-Bustos J., Heitman J., Hall M. N. Nuclear protein localization. Biochim Biophys Acta. 1991 Mar 7;1071(1):83–101. doi: 10.1016/0304-4157(91)90013-m. [DOI] [PubMed] [Google Scholar]
  7. Goday A., Sánchez-Martínez D., Gómez J., Puigdomènech P., Pagès M. Gene Expression in Developing Zea mays Embryos: Regulation by Abscisic Acid of a Highly Phosphorylated 23- to 25-kD Group of Proteins. Plant Physiol. 1988 Nov;88(3):564–569. doi: 10.1104/pp.88.3.564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hicks G. R., Raikhel N. V. Specific binding of nuclear localization sequences to plant nuclei. Plant Cell. 1993 Aug;5(8):983–994. doi: 10.1105/tpc.5.8.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hunter T., Karin M. The regulation of transcription by phosphorylation. Cell. 1992 Aug 7;70(3):375–387. doi: 10.1016/0092-8674(92)90162-6. [DOI] [PubMed] [Google Scholar]
  10. Jackson D., Culianez-Macia F., Prescott A. G., Roberts K., Martin C. Expression patterns of myb genes from Antirrhinum flowers. Plant Cell. 1991 Feb;3(2):115–125. doi: 10.1105/tpc.3.2.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. doi: 10.1016/0092-8674(84)90457-4. [DOI] [PubMed] [Google Scholar]
  12. Klimczak L. J., Schindler U., Cashmore A. R. DNA binding activity of the Arabidopsis G-box binding factor GBF1 is stimulated by phosphorylation by casein kinase II from broccoli. Plant Cell. 1992 Jan;4(1):87–98. doi: 10.1105/tpc.4.1.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Krek W., Maridor G., Nigg E. A. Casein kinase II is a predominantly nuclear enzyme. J Cell Biol. 1992 Jan;116(1):43–55. doi: 10.1083/jcb.116.1.43. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lee W. C., Mélèse T. Identification and characterization of a nuclear localization sequence-binding protein in yeast. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8808–8812. doi: 10.1073/pnas.86.22.8808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lee W. C., Xue Z. X., Mélèse T. The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J Cell Biol. 1991 Apr;113(1):1–12. doi: 10.1083/jcb.113.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lee W. C., Zabetakis D., Mélèse T. NSR1 is required for pre-rRNA processing and for the proper maintenance of steady-state levels of ribosomal subunits. Mol Cell Biol. 1992 Sep;12(9):3865–3871. doi: 10.1128/mcb.12.9.3865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Luthe D. S., Quatrano R. S. Transcription in Isolated Wheat Nuclei: I. ISOLATION OF NUCLEI AND ELIMINATION OF ENDOGENOUS RIBONUCLEASE ACTIVITY. Plant Physiol. 1980 Feb;65(2):305–308. doi: 10.1104/pp.65.2.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Meier U. T., Blobel G. A nuclear localization signal binding protein in the nucleolus. J Cell Biol. 1990 Dec;111(6 Pt 1):2235–2245. doi: 10.1083/jcb.111.6.2235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Meier U. T., Blobel G. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell. 1992 Jul 10;70(1):127–138. doi: 10.1016/0092-8674(92)90539-o. [DOI] [PubMed] [Google Scholar]
  20. Mundy J., Chua N. H. Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. 1988 Aug;7(8):2279–2286. doi: 10.1002/j.1460-2075.1988.tb03070.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Pla M., Gómez J., Goday A., Pagès M. Regulation of the abscisic acid-responsive gene rab28 in maize viviparous mutants. Mol Gen Genet. 1991 Dec;230(3):394–400. doi: 10.1007/BF00280296. [DOI] [PubMed] [Google Scholar]
  22. Plana M., Itarte E., Eritja R., Goday A., Pagès M., Martínez M. C. Phosphorylation of maize RAB-17 protein by casein kinase 2. J Biol Chem. 1991 Nov 25;266(33):22510–22514. [PubMed] [Google Scholar]
  23. Rihs H. P., Jans D. A., Fan H., Peters R. The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 1991 Mar;10(3):633–639. doi: 10.1002/j.1460-2075.1991.tb07991.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Silver P. A. How proteins enter the nucleus. Cell. 1991 Feb 8;64(3):489–497. doi: 10.1016/0092-8674(91)90233-o. [DOI] [PubMed] [Google Scholar]
  25. Skriver K., Mundy J. Gene expression in response to abscisic acid and osmotic stress. Plant Cell. 1990 Jun;2(6):503–512. doi: 10.1105/tpc.2.6.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Stochaj U., Silver P. A. A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import. J Cell Biol. 1992 May;117(3):473–482. doi: 10.1083/jcb.117.3.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Varagona M. J., Schmidt R. J., Raikhel N. V. Nuclear localization signal(s) required for nuclear targeting of the maize regulatory protein Opaque-2. Plant Cell. 1992 Oct;4(10):1213–1227. doi: 10.1105/tpc.4.10.1213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Vilardell J., Goday A., Freire M. A., Torrent M., Martínez M. C., Torné J. M., Pagès M. Gene sequence, developmental expression, and protein phosphorylation of RAB-17 in maize. Plant Mol Biol. 1990 Mar;14(3):423–432. doi: 10.1007/BF00028778. [DOI] [PubMed] [Google Scholar]
  29. Yamasaki L., Kanda P., Lanford R. E. Identification of four nuclear transport signal-binding proteins that interact with diverse transport signals. Mol Cell Biol. 1989 Jul;9(7):3028–3036. doi: 10.1128/mcb.9.7.3028. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. van der Krol A. R., Chua N. H. The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei. Plant Cell. 1991 Jul;3(7):667–675. doi: 10.1105/tpc.3.7.667. [DOI] [PMC free article] [PubMed] [Google Scholar]

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