Literature DB >> 24196924

Distribution of glucose/mannose-specific isolectins in pea (Pisum sativum L.) seedlings.

C L Díaz1, M Hosselet, G J Logman, E van Driessche, B J Lugtenberg, J W Kijne.   

Abstract

We report on the distribution and initial characterization of glucose/mannose-specific isolectins of 4- and 7-d-old pea (Pisum sativum L.) seedlings grown with or without nitrate supply. Particular attention was payed to root lectin, which probably functions as a determinant of host-plant specificity during the infection of pea roots by Rhizobium leguminosarum bv. viciae. A pair of seedling cotyledons yielded 545±49 μg of affinity-purified lectin, approx. 25% more lectin than did dry seeds. Shoots and roots of 4-d-old seedlings contained 100-fold less lectin than cotyledons, whereas only traces of lectin could be found in shoots and roots from 7-d-old seedlings. Polypeptides with a subunit structure similar to the precursor of the pea seed lectin could be demonstrated in cotyledons, shoots and roots. Chromatofocusing and isoelectric focusing showed that seed and non-seed isolectin differ in composition. An isolectin with an isoelectric point at pH 7.2 appeared to be a typical pea seed isolectin, whereas an isolectin focusing at pH 6.1 was the major non-seed lectin. The latter isolectin was also found in root cell-wall extracts, detached root hairs and root-surface washings. All non-seed isolectins were cross-reactive with rabbit antiserum raised against the seed isolectin with an isolectric point at pH 6.1. A protein similar to this acidic glucose/mannose-specific seed isolectin possibly represents the major lectin to be encountered by Rhizobium leguminosarum bv. viciae in the pea rhizosphere and at the root surface. Growth of pea seedlings in a nitrate-rich medium neither affected the distribution of isolectins nor their hemagglutination activity; however, the yield of affinity-purified root lectin was significantly reduced whereas shoot lectin yield slightly increased. Agglutination-inhibition tests demonstrated an overall similar sugar-binding specificity for pea seed and non-seed lectin. However root lectin from seedlings grown with or without nitrate supplement, and shoot lectin from nitrate-supplied seedlings showed a slightly different spectrum of sugar binding. The absorption spectra obtained by circular dichroism of seed and root lectin in the presence of a hapten also differed. These data indicate that nutritional conditions may affect the sugar-binding activity of non-seed isolectin, and that despite their similarities, seed and non-seed isolectins have different properties that may reflect tissue-specialization.

Entities:  

Year:  1990        PMID: 24196924     DOI: 10.1007/BF00192997

Source DB:  PubMed          Journal:  Planta        ISSN: 0032-0935            Impact factor:   4.116


  33 in total

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Authors:  P A Kaminski; D Buffard; A D Strosberg
Journal:  Plant Mol Biol       Date:  1987-09       Impact factor: 4.076

2.  Detection and characterization of a lectin from non-seed tissue ofPhaseolus vulgaris.

Authors:  C A Borrebaeck
Journal:  Planta       Date:  1984-05       Impact factor: 4.116

3.  Transcriptional and posttranscriptional regulation of seed storage-protein gene expression in pea (Pisum sativum L.).

Authors:  A J Thompson; I M Evans; D Boulter; R R Croy; J A Gatehouse
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Journal:  J Biol Chem       Date:  1973-01-25       Impact factor: 5.157

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Authors:  L Scopsi; L I Larsson
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6.  The biosynthesis and primary structure of pea seed lectin.

Authors:  T J Higgins; P M Chandler; G Zurawski; S C Button; D Spencer
Journal:  J Biol Chem       Date:  1983-08-10       Impact factor: 5.157

7.  Properties of Lectins in the Root and Seed of Lotononis bainesii.

Authors:  I J Law; B W Strijdom
Journal:  Plant Physiol       Date:  1984-04       Impact factor: 8.340

8.  Soybean lectin and related proteins in seeds and roots of le and le soybean varieties.

Authors:  L O Vodkin; N V Raikhel
Journal:  Plant Physiol       Date:  1986-06       Impact factor: 8.340

9.  A developmentally regulated bud specific transcript in pea has sequence similarity to seed lectins.

Authors:  M S Dobres; W F Thompson
Journal:  Plant Physiol       Date:  1989-03       Impact factor: 8.340

10.  Trifolin: a Rhizobium recognition protein from white clover.

Authors:  F B Dazzo; W E Yanke; W J Brill
Journal:  Biochim Biophys Acta       Date:  1978-03-20
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  7 in total

1.  Insertion of pea lectin into a phospholipid monolayer.

Authors:  P Booij; R A Demel; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1996-04       Impact factor: 4.076

2.  Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product.

Authors:  F J Hoedemaeker; M Richardson; C L Díaz; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1994-01       Impact factor: 4.076

3.  Photo-click immobilization on quartz crystal microbalance sensors for selective carbohydrate-protein interaction analyses.

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4.  Destabilization of pea lectin by substitution of a single amino acid in a surface loop.

Authors:  F J Hoedemaeker; R R van Eijsden; C L Díaz; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1993-09       Impact factor: 4.076

5.  Pea lectin is correctly processed, stable and active in leaves of transgenic potato plants.

Authors:  G A Edwards; A Hepher; S P Clerk; D Boulter
Journal:  Plant Mol Biol       Date:  1991-07       Impact factor: 4.076

6.  Sugar-binding activity of pea (Pisum sativum) lectin is essential for heterologous infection of transgenic white clover hairy roots by Rhizobium leguminosarum biovar viciae.

Authors:  R van Eijsden; C L Díaz; B S de Pater; J W Kijne
Journal:  Plant Mol Biol       Date:  1995-11       Impact factor: 4.076

7.  Purification and partial characterization of a glycoprotein from pea (Pisum sativum) with receptor activity for rhicadhesin, an attachment protein of Rhizobiaceae.

Authors:  S Swart; T J Logman; G Smit; B J Lugtenberg; J W Kijne
Journal:  Plant Mol Biol       Date:  1994-01       Impact factor: 4.076

  7 in total

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