Utilization of nitrate by bacteroids of Bradyrhizobium japonicum in the soybean root nodule

Planta ◽  
1988 ◽  
Vol 174 (1) ◽  
pp. 51-58 ◽  
Author(s):  
C. Giannakis ◽  
D. J. D. Nicholas ◽  
W. Wallace
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Root Nodule ◽  
Soybean Root

Bradyrhizobium Japonicum Genes Involved in Soybean Root-Nodule Development

1986 ◽  
pp. 79-86 ◽  
Author(s):  
Joseph W. Lamb ◽  
Brigitte Regensburger ◽  
Hans-Martin Fisher ◽  
Michael Göttfert ◽  
Linda Meyer ◽  
...  
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Root Nodule ◽  
Nodule Development ◽  
Soybean Root

Bradyrhizobium japonicum mutants defective in root-nodule bacteroid development and nitrogen fixation

1986 ◽  
Vol 144 (4) ◽  
pp. 355-366 ◽  
Author(s):  
B. Regensburger ◽  
L. Meyer ◽  
M. Filser ◽  
J. Weber ◽  
D. Studer ◽  
...  
Keyword(s):  
Nitrogen Fixation ◽  
Bradyrhizobium Japonicum ◽  
Root Nodule

scholarly journals Soybean root system under the effect of Bradyrhizobium japonicum

2018 ◽  
Vol 0 (1) ◽  
pp. 138-143
Author(s):  
Ірина Ігорівна Гуменюк ◽  
Сергій Юрійович Грузінський ◽  
Ірина Степанівна Бровко ◽  
Ярослав Васильович Чабанюк
Keyword(s):  
Root System ◽  
Bradyrhizobium Japonicum ◽  
Soybean Root

Studies on possible routes of ammonium assimilation in soybean root nodule bacteroids

1973 ◽  
Vol 19 (12) ◽  
pp. 1493-1499 ◽  
Author(s):  
Stanley D. Dunn ◽  
Robert V. Klucas
Keyword(s):  
Glutamine Synthetase ◽  
Nitrogen Assimilation ◽  
Reductive Amination ◽  
Root Nodule ◽  
Root Nodules ◽  
Ammonium Assimilation ◽  
Kinetic Properties ◽  
Transferase Activity ◽  
Soybean Root

Glutamine amide–2-oxoglutarate aminotransferase NAD+ oxidoreductase (GOGAT), glutamine synthetase (GS), glutamate dehydrogenase (GD), and alanine dehydrogenase (AD) were studied in soybean root nodules. GS, GOGAT, and AD were present in bacteroids at levels that could account for ammonium assimilation, but GD activity was quite low. The total activities of GS and GD were higher in the cytosol than in the bacteroids by factors of 20 and 7, respectively, whereas GOGAT was not detected in the cytosol. GS (transferase activity) was inhibited by alanine, CTP, glycine, and tryptophan at 5 mM but was relatively unaffected by asparagine, aspartic acid, CMP, glucosamine, and histidine at 5 mM. GOGAT activity was unaffected by ATP, ADP, 8-hydroxyquinoline, and 1,10-phenanthroline but was inhibited by EDTA, citrate, and parachloromercuribenzoate. GOGAT activity (reductive amination) was also inhibited 97% by preincubation with 10−4 M azaserine for 30 min but GD activity was inhibited only 13%. The apparent Km values for NH4+ by AD was 7.4 × 10−3 M and by GD was 7.3 × 10−2 M while for glutamine by GOGAT it was 9.3 × 10−5 M. Activities and kinetic properties for these enzymes may suggest potential routes of nitrogen assimilation in vivo.

scholarly journals Proteomic Analysis of Soybean Root Hairs After Infection by Bradyrhizobium japonicum

2005 ◽  
Vol 18 (5) ◽  
pp. 458-467 ◽  
Author(s):  
Jinrong Wan ◽  
Michael Torres ◽  
Ashwin Ganapathy ◽  
Jay Thelen ◽  
Beverly B. DaGue ◽  
...  
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Polyacrylamide Gel Electrophoresis ◽  
Root Hairs ◽  
Ionization Time ◽  
Soybean Root ◽  
Novel Proteins ◽  
Rhizobial Inoculation ◽  
Proteomic Study ◽  
Complex Events ◽  
Root Hair Infection

Infection of soybean root hairs by Bradyrhizobium japonicum is the first of several complex events leading to nodulation. In the current proteomic study, soybean root hairs after inoculation with B. japonicum were separated from roots. Total proteins were analyzed by two-dimensional (2-D) polyacrylamide gel electrophoresis. In one experiment, 96 protein spots were analyzed by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) to compare protein profiles between uninoculated roots and root hairs. Another 37 spots, derived from inoculated root hairs over different timepoints, were also analyzed by tandem MS (MS/MS). As expected, some proteins were differentially expressed in root hairs compared with roots (e.g., a chitinase and phosphoenolpyruvate carboxylase). Out of 37 spots analyzed by MS/MS, 27 candidate proteins were identified by database comparisons. These included several proteins known to respond to rhizobial inoculation (e.g., peroxidase and phenylalanine-ammonia lyase). However, novel proteins were also identified (e.g., phospholipase D and phosphoglucomutase). This research establishes an excellent system for the study of root-hair infection by rhizobia and, in a more general sense, the functional genomics of a single, plant cell type. The results obtained also indicate that proteomic studies with soybean, lacking a complete genome sequence, are practical.

scholarly journals Complete Transcriptome of the Soybean Root Hair Cell, a Single-Cell Model, and Its Alteration in Response to Bradyrhizobium japonicum Infection

2009 ◽  
Vol 152 (2) ◽  
pp. 541-552 ◽  
Author(s):  
Marc Libault ◽  
Andrew Farmer ◽  
Laurent Brechenmacher ◽  
Jenny Drnevich ◽  
Raymond J. Langley ◽  
...  
Keyword(s):  
Hair Cell ◽  
Single Cell ◽  
Root Hair ◽  
Bradyrhizobium Japonicum ◽  
Cell Model ◽  
Soybean Root ◽  
Root Hair Cell ◽  
Single Cell Model

scholarly journals pyd Genes of Rhizobium sp. Strain TAL1145 Are Required for Degradation of 3-Hydroxy-4-Pyridone, an Aromatic Intermediate in Mimosine Metabolism

2005 ◽  
Vol 187 (13) ◽  
pp. 4480-4487 ◽  
Author(s):  
Jonathan D. Awaya ◽  
Paul M. Fox ◽  
Dulal Borthakur
Keyword(s):  
Abc Transporter ◽  
Bradyrhizobium Japonicum ◽  
Sinorhizobium Meliloti ◽  
Root Nodule ◽  
Structural Genes ◽  
Nodule Bacteria ◽  
Mesorhizobium Loti ◽  
Root Nodule Bacteria ◽  
Low Levels ◽  
Rhizobium Sp

ABSTRACT Rhizobium sp. strain TAL1145 degrades the Leucaena toxin mimosine and its degradation product 3-hydroxy-4-pyridone (HP). The aim of this investigation is to characterize the Rhizobium genes for HP degradation and transport. These genes were localized by subcloning and mutagenesis on a previously isolated cosmid, pUHR263, containing mid genes of TAL1145 required for mimosine degradation. Two structural genes, pydA and pydB, encoding a metacleavage dioxygenase and a hydrolase, respectively, are required for degradation of HP, and three genes, pydC, pydD, and pydE, encoding proteins of an ABC transporter, are involved in the uptake of HP by TAL1145. These genes are induced by HP, although both pydA and pydB show low levels of expression without HP. pydA and pydB are cotranscribed, while pydC, pydD, and pydE are each transcribed from separate promoters. PydA and PydB show no homology with other dioxygenases and hydrolases in Sinorhizobium meliloti, Mesorhizobium loti, and Bradyrhizobium japonicum. Among various root nodule bacteria, the ability to degrade mimosine or HP is unique to some Leucaena-nodulating Rhizobium strains.

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