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. 1995 Oct;109(2):603–610. doi: 10.1104/pp.109.2.603

Targeting and release of phytohemagglutinin from the roots of bean seedlings.

S Kjemtrup 1, O Borkhsenious 1, N V Raikhel 1, M J Chrispeels 1
PMCID: PMC157626  PMID: 7480348

Abstract

Phytohemagglutinin (PHA), an abundant vacuolar seed protein of the common bean (Phaseolus vulgaris), is a tetramer of two homologous polypeptides, PHA-E and PHA-L. The roots of bean seedlings release into the culture medium a cross-reacting lectin that is most closely related to PHA-E. Reverse-transcriptase polymerase chain reaction with root mRNA as template was used to identify PHA transcripts in the roots of bean seedlings. Roots were found to contain mRNA for PHA-E but not for PHA-L. Indirect immunocytochemical detection with colloidal gold and antibodies to deglycosylated PHA showed that in the meristem of the primary root, PHA accumulates in vacuoles. However, in elongated root cells PHA was found only in the cell walls, indicating targeting to an alternate location. These results are discussed in relation to the various mechanisms that may account for the release of a normally vacuolar protein by roots.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bednarek S. Y., Raikhel N. V. The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell. 1991 Nov;3(11):1195–1206. doi: 10.1105/tpc.3.11.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bohlool B. B., Schmidt E. L. Lectins: a possible basis for specificity in the Rhizobium--legume root nodule symbiosis. Science. 1974 Jul 19;185(4147):269–271. doi: 10.1126/science.185.4147.269. [DOI] [PubMed] [Google Scholar]
  3. Chrispeels M. J., Raikhel N. V. Lectins, lectin genes, and their role in plant defense. Plant Cell. 1991 Jan;3(1):1–9. doi: 10.1105/tpc.3.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Felsted R. L., Leavitt R. D., Bachur N. R. Purification of the phytohemagglutinin family of proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatography. Biochim Biophys Acta. 1975 Sep 9;405(1):72–81. doi: 10.1016/0005-2795(75)90316-5. [DOI] [PubMed] [Google Scholar]
  5. Gade W., Jack M. A., Dahl J. B., Schmidt E. L., Wold F. The isolation and characterization of a root lectin from soybean (Glycine max (L), cultivar Chippewa). J Biol Chem. 1981 Dec 25;256(24):12905–12910. [PubMed] [Google Scholar]
  6. Hamblin J., Kent S. P. Possible role of phytohaemagglutinin in Phaseolus vulgaris L. Nat New Biol. 1973 Sep 5;245(140):28–30. doi: 10.1038/newbio245028a0. [DOI] [PubMed] [Google Scholar]
  7. Hoedemaeker F. J., Richardson M., Díaz C. L., de Pater B. S., Kijne J. W. Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product. Plant Mol Biol. 1994 Jan;24(1):75–81. doi: 10.1007/BF00040575. [DOI] [PubMed] [Google Scholar]
  8. Hoffman L. M., Donaldson D. D. Characterization of two Phaseolus vulgaris phytohemagglutinin genes closely linked on the chromosome. EMBO J. 1985 Apr;4(4):883–889. doi: 10.1002/j.1460-2075.1985.tb03714.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Höfte H., Chrispeels M. J. Protein sorting to the vacuolar membrane. Plant Cell. 1992 Aug;4(8):995–1004. doi: 10.1105/tpc.4.8.995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Laurière M., Laurière C., Chrispeels M. J., Johnson K. D., Sturm A. Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol. 1989 Jul;90(3):1182–1188. doi: 10.1104/pp.90.3.1182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rothman J. H., Hunter C. P., Valls L. A., Stevens T. H. Overproduction-induced mislocalization of a yeast vacuolar protein allows isolation of its structural gene. Proc Natl Acad Sci U S A. 1986 May;83(10):3248–3252. doi: 10.1073/pnas.83.10.3248. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Sharon N., Lis H. Legume lectins--a large family of homologous proteins. FASEB J. 1990 Nov;4(14):3198–3208. doi: 10.1096/fasebj.4.14.2227211. [DOI] [PubMed] [Google Scholar]
  13. Stevens T. H., Rothman J. H., Payne G. S., Schekman R. Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J Cell Biol. 1986 May;102(5):1551–1557. doi: 10.1083/jcb.102.5.1551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sturm A., Chrispeels M. J. The high mannose oligosaccharide of phytohemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60. Plant Physiol. 1986 May;81(1):320–322. doi: 10.1104/pp.81.1.320. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. VandenBosch K. A., Rodgers L. R., Sherrier D. J., Kishinevsky B. D. A Peanut Nodule Lectin in Infected Cells and in Vacuoles and the Extracellular Matrix of Nodule Parenchyma. Plant Physiol. 1994 Feb;104(2):327–337. doi: 10.1104/pp.104.2.327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Vitale A., Ceriotti A., Bollini R., Chrispeels M. J. Biosynthesis and processing of phytohemagglutinin in developing bean cotyledons. Eur J Biochem. 1984 May 15;141(1):97–104. doi: 10.1111/j.1432-1033.1984.tb08162.x. [DOI] [PubMed] [Google Scholar]
  17. Vodkin L. O., Raikhel N. V. Soybean lectin and related proteins in seeds and roots of le and le soybean varieties. Plant Physiol. 1986 Jun;81(2):558–565. doi: 10.1104/pp.81.2.558. [DOI] [PMC free article] [PubMed] [Google Scholar]

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