Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles

Plant Cell

Volumn 10, Issue 5, 1998, Pages 825-836

  Hara Nishimura, Ikuko ^a,b   Shimada, Tomoo ^a   Hatano, Kyoko ^a,c   Takeuchi, Yuka ^a   Nishimura, Mikio ^a,b  

^a NATIONAL INSTITUTE FOR BASIC BIOLOGY   (Japan)

^b GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

^c Kyoto University   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0031795695     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.10.5.825     Document Type: Article

References (49)

1. Ahmed, S.U., Bar-Peled, M., and Raikhel, N.V. (1997). Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein sorting receptors of eukaryotic cells. Plant Physiol. 114, 325-336.
2. Becherer, K.A., Rieder, S.E., Emr, S.D., and Jones, E.W. (1996). A novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast. Mol. Cell Biol. 7, 579-594.
3. Chrispeels, M.J. (1983). The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta 158, 140-151.
4. Chrispeels, M.J. (1985). The role of the Golgi apparatus in the transport and post-translational modification of vacuolar (protein body) proteins. Oxf. Surv. Plant Mol. Cell Biol. 2, 43-68.
5. Craig, S. (1988). Structural aspects of protein accumulation in developing legume seeds. Biochem. Physiol. Pflanz. 183, 159-171.
6. da Silva Conceição, A., Marty-Mazars, D., Bassham, D.C., Sanderfoot, A.A., Marty, F., and Raikhel, N.V. (1997). The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in plants. Plant Cell 9, 571-582.
7. Freund, J. (1951). The effect of paraffin oil and mycobacteria on antibody formation and sensitization. Am. J. Clin. Pathol. 21, 645-656.
8. Fukasawa, T., Hara-Nishimura, I., and Nishimura, M. (1988). Biosynthesis, intracellular transport and in vitro processing of 11S globulin precursor proteins of developing castor bean endosperm. Plant Cell Physiol. 29, 339-345.
9. Hara, I., and Matsubara, H. (1980). Pumpkin (Cucurbita sp.) seed globulin. VII. Immunofluorescent study on protein bodies in ungerminated and germinating cotyledon celts. Plant Cell Physiol. 21, 247-254.
10. Hara-Nishimura, I. (1987). Introduction of disulfide bond in proglobulin molecules during the 11S globulin biosynthesis in endoplasmic reticulum of developing pumpkin cotyledons. Agric. Biol. Chem. 61, 2007-2008.
11. Hara-Nishimura, I., and Nishimura, M. (1987). Proglobulin processing enzyme in vacuoles isolated from developing pumpkin cotyledons. Plant Physiol. 85, 440-445.
12. Hara-Nishimura, I., Nishimura, M., Matsubara, H., and Akazawa, T. (1982). Suborganellar localization of proteinase catalyzing the limited hydrolysis of pumpkin globulin. Plant Physiol. 70, 699-703.
13. Hara-Nishimura, I., Nishimura, M., and Akazawa, T. (1985). Biosynthesis and intracellular transport of 11S globulin in developing pumpkin cotyledons. Plant Physiol. 77, 747-752.
14. Hara-Nishimura, I., Hayashi, M., Nishimura, M., and Akazawa, T. (1987). Biogenesis of protein bodies by budding from vacuoles in developing pumpkin cotyledons. Protoplasma 136, 49-55.
15. Hara-Nishimura, I., Inoue, K., and Nishimura, M. (1991). A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett. 294, 89-93.
16. Hara-Nishimura, I., Takeuchi, Y., Inoue, K., and Nishimura, M. (1993a). Vesicle transport and processing of the precursor to 2S albumin in pumpkin. Plant J. 4, 793-800.
17. Hara-Nishimura, I., Takeuchi, Y., and Nishimura, M. (1993b). Molecular characterization of a vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. Plant Cell 5, 1651-1659.
18. Hara-Nishimura, I., Shimada, T., Hiraiwa, N., and Nishimura, M. (1995). Vacuolar processing enzyme responsible for maturation of seed proteins. J. Plant Physiol. 145, 632-640.
19. Hatano, K., Shimada, T., Hiraiwa, N., Nishimura, M., and Hara-Nishimura, I. (1997). A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons. Plant Cell Physiol. 38, 344-351.
20. Hayashi, M., Akazawa, T., Nishimura, M., and Hara-Nishimura, I. (1988). Effect of monensin on intracellular transport and posttranslational processing of 11S globulin precursors in developing pumpkin cotyledons. FEBS Lett. 238, 197-200.
21. Heupke, H.-J., and Robinson, D.G. (1985). Intracellular transport of α-amylase in barley aleurone cells: Evidence for the participation of the Golgi apparatus. Eur. J. Cell Biol. 39, 265-272.
22. Hiraiwa, N., Takeuchi, Y., Nishimura, M., and Hara-Nishimura, I. (1993). A vacuolar processing enzyme in maturing and germinating seeds: Its distribution and associated changes during development. Plant Cell Physiol. 34, 1197-1204.
23. Hiraiwa, N., Kondo, M., Nishimura, M., and Hara-Nishimura, I. (1997a). An aspartic proteinase is involved in the maturation of storage proteins in concert with the vacuolar processing enzyme. Eur. J. Biochem. 246, 133-141.
24. Hiraiwa, N., Nishimura, M., and Hara-Nishimura, I. (1997b). Expression and activation of the vacuolar processing enzyme in Saccharomyces cerevisiae. Plant J. 12, 819-829.
25. Hohl, I., Robinson, D.G., Chrispeels, M.J., and Hinz, G. (1996). Transport of storage proteins to the vacuole is mediated by vesicles without clathrin coat. J. Cell Sci. 109, 2539-2550.
26. Inoue, K., Motozaki, A., Takeuchi, Y., Nishimura, M., and Hara-Nishimura, I. (1995a). Molecular characterization of proteins in protein-body membranes that disappear most rapidly during transformation of protein bodies into vacuoles. Plant J. 7, 235-243.
27. Inoue, K., Takeuchi, Y., Nishimura, M., and Hara-Nishimura, I. (1995b). Characterization of two integral membrane proteins located in the protein bodies of pumpkin seeds. Plant Mol. Biol. 28, 1089-1101.
28. Kirsch, T., Paris, N., Butler, J.M., Beevers, L., and Rogers, J. (1994). Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc. Natl. Acad. Sci. USA 91, 3403-3407.
29. Larkins, B.A., and Hurkman, W.J. (1978). Synthesis and deposition of protein bodies of maize endosperm. Plant Physiol. 62, 256-263.
30. Levanony, H., Rubin, R., Altschuler, Y., and Galili, G. (1992). Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119, 1117-1128.
31. Li, X., Wu, Y., Zhang, D.-Z., Gillikin, J.W., Boston, R.S., Franceschi, V.R., and Okita, T.W. (1993). Rice prolamine protein body biogenesis: A BiP-mediated process. Science 262, 1054-1056.
32. +-ATPase during reformation of the central vacuole in germinating pumpkin seeds. Plant Physiol. 106, 61-69.
33. Mitsui, T., Akazawa, T., Christeller, J.T., and Tartakoff, A.M. (1985). Biosynthesis of rice seed α-amylase: Two pathways of amylase secretion by the scutellum. Arch. Biochem. Biophys. 241, 315-328.
34. Nishimura, M., Takeuchi, Y., De Bellis, L., and Hara-Nishimura, I. (1993). Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma 175, 131-137.
35. Okita, T.W., and Rogers, J.C. (1996). Compartmentation of proteins in the endomembrane system of plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 327-350.
36. Paris, N., Stanley, C.M., Jones, R.L., and Rogers, J.C. (1996). Plant cells contain two functionally distinct vacuolar compartments. Cell 85, 563-572.
37. Paris, N., Rogers, S.W., Jiang, L., Kirsch, T., Beevers, L., Philips, T.E., and Rogers, J.C. (1997). Molecular cloning and further characterization of a probable plant vacuolar sorting receptor. Plant Physiol. 115, 29-39.
38. Pryer, N.K., Wuestehube, L.J., and Schekman, R. (1992). Vesicle-mediated protein sorting. Annu. Rev. Biochem. 61, 471-516.
39. Robinson, D.G. (1996). Clathrin-mediated trafficking. Trends Plant Sci. 1, 349-355.
40. Robinson, D.G., and Hinz, G. (1996). Multiple mechanisms of protein body formation in pea cotyledons. Plant Physiol. Biochem. 34, 155-163.
41. Robinson, D.G., Hoh, B., Hinz, G., and Jeong, B.-K. (1995). One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development? J. Plant Physiol. 145, 654-664.
42. Sato, M.H., Nakamura, N., Ohsumi, Y., Kouchi, H., Kondo, M., Hara-Nishimura, I., Nishimura, M., and Wada, Y. (1997). The AtVAM3 encodes a syntaxin-related molecule implicated in the vacuolar assembly in Arabidopsis thaliana. J. Biol. Chem. 272, 24530-24535.
43. Shimada, T., Hiraiwa, N., Nishimura, M., and Hara-Nishimura, I. (1994a). Vacuolar processing enzyme of soybean that converts proprotein to the corresponding mature forms. Plant Cell Physiol. 35, 713-718.
44. Shimada, T., Nishimura, M., and Hara-Nishimura, I. (1994b). Small GTP-binding proteins are associated with the vesicles targeting to vacuoles in developing pumpkin cotyledons. Plant Cell Physiol. 35, 995-1001.
45. Shimada, T., Kuroyanagi, M., Nishimura, M., and Hara-Nishimura, I. (1997). Pumpkin 72-kDa membrane protein of precursor accumulating vesicles have characteristics for a vacuolar sorting receptor. Plant Cell Physiol. 38, 1414-1420.
46. Shotwell, M.A., and Larkins, B.A. (1988). The biochemistry and molecular biology of seed storage proteins. In The Biochemistry of Plants, B.J. Miflin, ed (New York: Academic Press), pp. 297-345.
47. Strzalka, K., Hara-Nishimura, I., and Nishimura, M. (1995). Changes in physical properties of vacuolar membrane during transformation of protein bodies into vacuoles in germinating pumpkin seeds. Biochim. Biophys. Acta 1239, 103-110.
48. Tezuka, K., Hayashi, M., Ishihara, H., Nishimura, M., Onozaki, K., and Takahashi, N. (1993). Purification and substrate specificity of β-xylosidase from sycamore cell (Acer pseudoplatanus L.): Application for structural analysis of xylose-containing N-linked oligosaccharides. Anal. Biochem. 211, 205-209.
49. Van der Wilden, W., Herman, E.M., and Chrispeels, M.J. (1980). Protein bodies of mung bean cotyledons as autophagic organelles. Proc. Natl. Acad. Sci. USA 77, 428-432.