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Plant Cell. 1994 Mar; 6(3): 351–360.
PMCID: PMC160438

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


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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  • Adam SA, Lobl TJ, Mitchell MA, Gerace L. Identification of specific binding proteins for a nuclear location sequence. Nature. 1989 Jan 19;337(6204):276–279. [PubMed]
  • 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. [PubMed]
  • Coen ES, Romero JM, 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. [PubMed]
  • Dure L., 3rd A repeating 11-mer amino acid motif and plant desiccation. Plant J. 1993 Mar;3(3):363–369. [PubMed]
  • Forbes DJ. Structure and function of the nuclear pore complex. Annu Rev Cell Biol. 1992;8:495–527. [PubMed]
  • Garcia-Bustos J, Heitman J, Hall MN. Nuclear protein localization. Biochim Biophys Acta. 1991 Mar 7;1071(1):83–101. [PubMed]
  • 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. [PMC free article] [PubMed]
  • Hicks GR, Raikhel NV. Specific binding of nuclear localization sequences to plant nuclei. Plant Cell. 1993 Aug;5(8):983–994. [PMC free article] [PubMed]
  • Hunter T, Karin M. The regulation of transcription by phosphorylation. Cell. 1992 Aug 7;70(3):375–387. [PubMed]
  • Jackson D, Culianez-Macia F, Prescott AG, Roberts K, Martin C. Expression patterns of myb genes from Antirrhinum flowers. Plant Cell. 1991 Feb;3(2):115–125. [PMC free article] [PubMed]
  • Kalderon D, Roberts BL, Richardson WD, Smith AE. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. [PubMed]
  • Klimczak LJ, Schindler U, Cashmore AR. 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. [PMC free article] [PubMed]
  • Krek W, Maridor G, Nigg EA. Casein kinase II is a predominantly nuclear enzyme. J Cell Biol. 1992 Jan;116(1):43–55. [PMC free article] [PubMed]
  • Lee WC, 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. [PMC free article] [PubMed]
  • Lee WC, Xue ZX, 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. [PMC free article] [PubMed]
  • Lee WC, 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. [PMC free article] [PubMed]
  • Luthe DS, Quatrano RS. Transcription in Isolated Wheat Nuclei: I. ISOLATION OF NUCLEI AND ELIMINATION OF ENDOGENOUS RIBONUCLEASE ACTIVITY. Plant Physiol. 1980 Feb;65(2):305–308. [PMC free article] [PubMed]
  • Meier UT, Blobel G. A nuclear localization signal binding protein in the nucleolus. J Cell Biol. 1990 Dec;111(6 Pt 1):2235–2245. [PMC free article] [PubMed]
  • Meier UT, Blobel G. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell. 1992 Jul 10;70(1):127–138. [PubMed]
  • Mundy J, Chua NH. Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. 1988 Aug;7(8):2279–2286. [PMC free article] [PubMed]
  • 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. [PubMed]
  • Plana M, Itarte E, Eritja R, Goday A, Pagès M, Martínez MC. Phosphorylation of maize RAB-17 protein by casein kinase 2. J Biol Chem. 1991 Nov 25;266(33):22510–22514. [PubMed]
  • Rihs HP, Jans DA, 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. [PMC free article] [PubMed]
  • Silver PA. How proteins enter the nucleus. Cell. 1991 Feb 8;64(3):489–497. [PubMed]
  • Skriver K, Mundy J. Gene expression in response to abscisic acid and osmotic stress. Plant Cell. 1990 Jun;2(6):503–512. [PMC free article] [PubMed]
  • Stochaj U, Silver PA. A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import. J Cell Biol. 1992 May;117(3):473–482. [PMC free article] [PubMed]
  • van der Krol AR, Chua NH. 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. [PMC free article] [PubMed]
  • Varagona MJ, Schmidt RJ, Raikhel NV. Nuclear localization signal(s) required for nuclear targeting of the maize regulatory protein Opaque-2. Plant Cell. 1992 Oct;4(10):1213–1227. [PMC free article] [PubMed]
  • Vilardell J, Goday A, Freire MA, Torrent M, Martínez MC, Torné JM, Pagès M. Gene sequence, developmental expression, and protein phosphorylation of RAB-17 in maize. Plant Mol Biol. 1990 Mar;14(3):423–432. [PubMed]
  • Yamasaki L, Kanda P, Lanford RE. Identification of four nuclear transport signal-binding proteins that interact with diverse transport signals. Mol Cell Biol. 1989 Jul;9(7):3028–3036. [PMC free article] [PubMed]

Articles from The Plant Cell are provided here courtesy of American Society of Plant Biologists


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