Selective trafficking of KNOTTED1 homeodomain protein and its mRNA through plasmodesmata

Science

Volumn 270, Issue 5244, 1995, Pages 1980-1983

  Lucas, William J ^a   Bouché Pillon, Sabine ^a   Jackson, David P ^b   Nguyen, Lynda ^a   Baker, Lucian ^a   Ding, Biao ^a,c   Hake, Sarah ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b PLANT GENE EXPRESSION CENTER   (United States)

^c OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HOMEODOMAIN PROTEIN; MESSENGER RNA; TRANSCRIPTION FACTOR;

CELL COMMUNICATION; CELL MEMBRANE TRANSPORT; CELL ORGANELLE; MICROINJECTION; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN TRANSPORT; SHORT SURVEY;

EID: 0029550602     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.270.5244.1980     Document Type: Short Survey

References (31)

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3. W. J. Lucas, Curr. Opin. Cell Biol. 7, 673 (1995).
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6. E. J. Symkowiak and I. M. Sussex, Plant Cell 4, 1089 (1992).
7. W. J. Lucas, B. Ding, C. Van der School, New Phytol. 125, 435 (1993); W. J. Lucas and S. Wolf, Trends Cell Biol. 3, 308 (1993).
8. W. J. Lucas, B. Ding, C. Van der School, New Phytol. 125, 435 (1993); W. J. Lucas and S. Wolf, Trends Cell Biol. 3, 308 (1993).
9. W. J. Lucas and R. L. Gilbertson, Annu. Rev. Phytopathol. 32, 387 (1994).
10. T. Fujiwara, D. Giesman-Cookmeyer, B. Ding, S. A. Lommel, W. J. Lucas, Plant Cell 5, 1783 (1993); A. O. Noueiry, W. J. Lucas, R. L. Gilbertson, Cell 76, 925 (1994); E. Waigmann, W. J. Lucas, V. Citovsky, P. Zambryski, Proc. Natl. Acad. Sci. U.S.A. 91, 1433 (1994).
11. T. Fujiwara, D. Giesman-Cookmeyer, B. Ding, S. A. Lommel, W. J. Lucas, Plant Cell 5, 1783 (1993); A. O. Noueiry, W. J. Lucas, R. L. Gilbertson, Cell 76, 925 (1994); E. Waigmann, W. J. Lucas, V. Citovsky, P. Zambryski, Proc. Natl. Acad. Sci. U.S.A. 91, 1433 (1994).
12. T. Fujiwara, D. Giesman-Cookmeyer, B. Ding, S. A. Lommel, W. J. Lucas, Plant Cell 5, 1783 (1993); A. O. Noueiry, W. J. Lucas, R. L. Gilbertson, Cell 76, 925 (1994); E. Waigmann, W. J. Lucas, V. Citovsky, P. Zambryski, Proc. Natl. Acad. Sci. U.S.A. 91, 1433 (1994).
13. B. Ding, L. Qiubo, L. Nguyen, P. Palukaitis, W. J. Lucas, Virology 207, 345 (1995).
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18. In situ hybridization and immunolocalization experiments were performed on paraffin-embedded maize seedling apices. In situ hybridization was performed exactly as described (11), whereas for immunolocalization we used the method of Smith et al. (9), except that tissue was embedded in paraffin wax and sections were predigested with proteinase K (Sigma) at 100 μg/ml in phosphate-buffered saline (PBS) for 10 min at room temperature and then rinsed twice in PBS before the blocking step. Goat antibody to rabbit alkaline phosphatase (Boehringer Mannheim) was used as the secondary antibody (1:600 dilution) and visualized according to the method of Jackson et al. (11). Sections were lightly counterstained in basic fuchsin (0.005% w/v).
19. D. Jackson, B. Veit, S. Hake, Development 120, 405 (1994).
20. Wild-type and mutant KN1 were expressed, extracted, and labeled with FITC according to the procedures we developed for viral movement proteins (7, 8). As an internal control, proteins were extracted and FITC-labeled from an an E. coli preparation that did not contain the kn1 complementary DNA (cDNA). Alanine scanning mutants were created in groups of charged amino acids, which are likely to be present in surface domains (PC gene software, Intelligenetics). The kn1 cDNA (Bam HI-Nco I partial digest) from pKOC10 was inserted into the pET23-d(+) vector (Novagen) to create pDJX-1. Single-stranded virions were produced in the CJ236 (dut ung) strain of E. coli, and site-directed mutagenesis was performed with oligonucleotides of 33 to 48 bases and with T7 DNA polymerase, according to the manufacturer's instructions (U.S. Biochemical). Mutagenized clones were confirmed by being sequenced before transfer to strain BL21 (DE3) for protein production.
21. Microinjections were carried out essentially as previously described [S. Wolf, C. M. Deom, R. N. Beachy, W. J. Lucas, Science 246, 377 (1989)], except for the modifications noted in (7, 8).
22. N. Sinha, R. Williams, S. Hake, Genes Dev. 7, 787 (1993).
23. A. W. Robards and W. J. Lucas, Annu. Rev. Plant Physiol. Plant Molec. Biol. 41, 369 (1990).
24. E. Vollbrecht, R. Kerstetter, B. Lowe, B. Veit, S. Hake, in Evolutionary Conservation of Developmental Mechanisms, A. C. Spalding, Ed. (Wiley-Liss, New York, 1993), pp. 111-123; R. Kerstetter et al., Plant Cell 6, 1877 (1994); C. Lincoln, J. Long, J. Yamaguchi, K. Serikawa, S. Hake, ibid., p. 1859.
25. E. Vollbrecht, R. Kerstetter, B. Lowe, B. Veit, S. Hake, in Evolutionary Conservation of Developmental Mechanisms, A. C. Spalding, Ed. (Wiley-Liss, New York, 1993), pp. 111-123; R. Kerstetter et al., Plant Cell 6, 1877 (1994); C. Lincoln, J. Long, J. Yamaguchi, K. Serikawa, S. Hake, ibid., p. 1859.
26. E. Vollbrecht, R. Kerstetter, B. Lowe, B. Veit, S. Hake, in Evolutionary Conservation of Developmental Mechanisms, A. C. Spalding, Ed. (Wiley-Liss, New York, 1993), pp. 111-123; R. Kerstetter et al., Plant Cell 6, 1877 (1994); C. Lincoln, J. Long, J. Yamaguchi, K. Serikawa, S. Hake, ibid., p. 1859.
27. 2O, and concentration and purity were determined by spectroscopy. Sense and antisense RNA (500 μg/ ml) were labeled with the nucleotide-specific fluorescent probe TOTO-1 (Molecular Probes) as previously described (7, 8). All kn1 RNA-TOTO preparations were adjusted to 225 μg/ml for use in microinjection experiments. CMV RNA-TOTO was adjusted to 250 to 500 μg/ml.
28. Purified CMV RNA was prepared [P. Palukaitis and M. Zaitlin, Virology 132, 426 (1984)] and TOTO-labeled as described by Ding et al. (8). This preparation contained three single-stranded RNA species, RNA1 (3.3 kb), RNA2 (3.0 kb), and RNA3 (2.2 kb). The procedures of Ding et al. (8) were used to prepare and FITC-label the CMV 3a movement protein.
29. P. W. Becraft and M. Freeling, Genetics 136, 295 (1994).
30. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, GLu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
31. We thank P. Palukaitis of Cornell University for providing us with CMV RNA and the clone expressing the CMV 3a movement protein and M. Pfitzner for technical assistance with the color illustrations. Supported by NSF grant IBN-9406974 (W.J.L) and U.S. Department of Agriculture CRIS 5335-21000-007-0OD (S.H.).