Literature DB >> 24178068

Chitinase and peroxidase in effective (fix(+)) and ineffective (fix (-)) soybean nodules.

C Staehelin1, J Müller, R B Mellor, A Wiemken, T Boller.   

Abstract

Chitinase and peroxidase, two enzymes thought to be involved in the defense of plants against pathogens, were measured in soybean (Glycine max L. Merr.) roots and in nodules colonized by Bradyrhizobium japonicum strains differing in their symbiotic potential. Activities of both enzymes were higher in nodules than in roots. In "effective", nitrogen-fixing nodules, colonized by wild-type bacteria, chitinase and peroxidase activities had low levels in the central infected zone and were enhanced primarily in the nodule cortex. An ascorbate-specific peroxidase, possibly involved in radical scavenging, had similarly high activities in the infected zone and in the cortex. "Ineffective" nodules colonized by bacteria unable to fix nitrogen symbiotically showed a similar distribution of chitinase and peroxidase. In another type of "ineffective" nodule, colonized by a B. japonicum strain eliciting a hypersensitive response, activities of both enzymes were enhanced to a similar degree in the infected zone as well as in the cortex. Tissue prints using a direct assay for peroxidase and an antiserum against bean chitinase corroborated these results. The antiserum against bean chitinase cross-reacted with a nodule protein of Mr 32 000; it inhibited most of the chitinase activity in the nodules but barely affected the chitinase in uninfected roots. It is concluded that proteins characteristic of the defense reaction accumulate in the cortex of nodules independently of their ability to fix nitrogen, and in the entire body of hypersensitively reacting nodules.

Entities:  

Year:  1992        PMID: 24178068     DOI: 10.1007/BF00195651

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


  20 in total

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Review 5.  Rhizobium infection and nodulation: a beneficial plant disease?

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6.  Lysis of bacterioids in the vicinity of the host cell nucleus in an ineffective (fix(-)) root nodule of soybean (Glycine max).

Authors:  D Werner; E Mörschel; R Kort; R B Mellor; S Bassarab
Journal:  Planta       Date:  1984-09       Impact factor: 4.116

7.  Purification, properties, and distribution of ascorbate peroxidase in legume root nodules.

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Journal:  Nature       Date:  1990-04-19       Impact factor: 49.962

9.  A novel highly unsaturated fatty acid moiety of lipo-oligosaccharide signals determines host specificity of Rhizobium.

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Journal:  Nature       Date:  1991-11-14       Impact factor: 49.962

10.  Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function.

Authors:  T Boller; A Gehri; F Mauch; U Vögeli
Journal:  Planta       Date:  1983-02       Impact factor: 4.116

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  8 in total

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Journal:  Plant Cell       Date:  2018-01-24       Impact factor: 11.277

5.  Sinorhizobium meliloti-induced chitinase gene expression in Medicago truncatula ecotype R108-1: a comparison between symbiosis-specific class V and defence-related class IV chitinases.

Authors:  Peter Salzer; Nadja Feddermann; Andres Wiemken; Thomas Boller; Christian Staehelin
Journal:  Planta       Date:  2004-04-24       Impact factor: 4.116

6.  Symbiosis-promoting and deleterious effects of NopT, a novel type 3 effector of Rhizobium sp. strain NGR234.

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7.  NopL, an effector protein of Rhizobium sp. NGR234, thwarts activation of plant defense reactions.

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Journal:  Plant Physiol       Date:  2004-02       Impact factor: 8.340

8.  The nodulation factor hydrolase of Medicago truncatula: characterization of an enzyme specifically cleaving rhizobial nodulation signals.

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  8 in total

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