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Rhizobium leguminosarum sulfoquinovose metabolism

ABSTRACT: LFQ analysis of Whole bacterial lysates of Rhizobium leguminosarum growth with and with sulfoquinovose.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Rhizobium Cf. Leguminosarum

SUBMITTER: Nichollas Scott

LAB HEAD: Spencer Williams

PROVIDER: PXD015822 | Pride | 2020-05-25

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	Maxqaunt_outputs.zip	Other
	Nsco_20190809_SW_SQ_RL_M_B1.raw	Raw
	Nsco_20190809_SW_SQ_RL_M_B2.raw	Raw
	Nsco_20190809_SW_SQ_RL_M_B3.raw	Raw
	Nsco_20190809_SW_SQ_RL_M_B4.raw	Raw

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Publications

A Sulfoglycolytic Entner-Doudoroff Pathway in Rhizobium leguminosarum bv. trifolii SRDI565.

Li Jinling J Epa Ruwan R Scott Nichollas E NE Skoneczny Dominik D Sharma Mahima M Snow Alexander J D AJD Lingford James P JP Goddard-Borger Ethan D ED Davies Gideon J GJ McConville Malcolm J MJ Williams Spencer J SJ

Applied and environmental microbiology 20200720 15

Rhizobia are nitrogen-fixing bacteria that engage in symbiotic relationships with plant hosts but can also persist as free-living bacteria in the soil and rhizosphere. Here, we show that free-living <i>Rhizobium leguminosarum</i> SRDI565 can grow on the sulfosugar sulfoquinovose (SQ) or the related glycoside SQ-glycerol using a sulfoglycolytic Entner-Doudoroff (sulfo-ED) pathway, resulting in production of sulfolactate (SL) as the major metabolic end product. Comparative proteomics supports the ...[more]

PMID: 32444469

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Isolation and characterisation of a 14kDa adhesin protein from Rhizobium leguminosarum biovar viciae 3841

Project description:In this project we aimed to identify a 14 kDa adhesin protein from Rhizobium leguminosarum biovar viciae 3841 unsing in gel digestion coupled to LC-MS/MS.

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Antioxidant mechanism of glutaredoxins and their role in symbiotic nitrogen fixation in Rhizobium leguminosarum bv. viciae 3841

Project description:Glutaredoxins (Grx) are redoxin family proteins that reduce disulfifides and mixed disulfifides between glutathione and proteins. Rhizobium leguminosarum 3841 contains three genes coding for glutaredoxins: RL4289 (grxA) codes for a dithiolic glutaredoxin, RL2615 (grxB) codes for a monothiol glutaredoxin, while RL4261 (grxC) codes for a glutaredoxin-like NrdH protein. In this study, we have generated mutants which have interrupted one, two, or three glutaredoxin genes. These mutants had no different growth phenotypes from the wild type RL3841. Mutation of grxC did not affect R. leguminosarum antioxidant or symbiotic capacities, while grxA-derived or grxB-derived mutants decreased the antioxidant and fixation nitrogen capacity. grxA-derived mutants was severely impaired in there rhizosphere colonization, and formed maller nodules with defects of bacteroid differentiation. whereas nodules induced by grxB-derived mutants contained abnormally thick cortexs and prematurely senescent bacteroids. Surprisingly the grx triple mutant presented an enhanced defect in antioxidant and symbiotic capacities of R. leguminosarum. LC-MS/MS analysis quantitative proteomics techniques were employed to compare differential grx triple mutant root bacteroids in response to the wild type infection. 137 differentially expressed proteins were identified including 56 up-regulated and 81 down-regulated proteins. By sorting the identified proteins according to metabolic function, twenty-eight proteins were involved in transporter activity, twenty proteins were related to stress response and virulence, and sixteen proteins were related to amino acid metabolism. Overall, R. leguminosarum glutaredoxins play an important role in root nodule symbiosis by involving the functions of anti-oxidant defenses, Fe-S cluster assembly, and control of bacteroid differentiation and senescence.

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Project description:Glutathione plays a tremendous role in regulating the homeostasis of redox state, and appears to be essential for proper development of the root nodules. Glutathione peroxidase catalyzes the reduction of peroxides by oxidation of GSH to oxidized GSH (GSSG), which can in turn be reduced by glutathione reductase (GR). However, it has not been determined whether the R. leguminosarum Gpx or GR is required during symbiotic interactions with pea. To characterise the role of glutathione-dependent enzymes in the symbiotic process, single and double mutants were made in gpxA and gorA genes. All the mutations did not affect the growth of R. leguminosarum, but they increased the sensitivity of R. leguminosarum strains to H2O2. The gorA mutant can induce the formation of normal nodules, while the gpxA single and double mutants exhibited an abnormal nodulation phenotype coupled to more than 50% reduction in nitrogen-fifixing capacity, this defect in nodulation was characterized by the formation of undeveloped and ineffective nodules. In addition, the gorA and gpxA double mutant was severely impaired in rhizosphere colonization. LC-MS/MS analysis quantitative proteomics techniques were employed to compare differential gpxA mutant root bacteroids in response to the wild type infection. Sixty differentially expressed proteins were identified including seven up-regulated and twenty down-regulated proteins. By sorting the down-regulated proteins according to metabolic function, eight proteins were transporter protein, seven proteins were dehydrogenases and deoxygenases. Moreover, three down-regulation proteins are directly involved in nodule process.

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Transcription profiling of Rhizobium leguminosarum biovar viciae strain 3841 grown on acetate versus glucose

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Transcription profiling by array of Rhizobium leguminosarum Rlv 3841 grown on glucose ammonia with and without the flavonoid hesperitin

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Transcription profiling of Rhizobium leguminosarum biovar viciae grown on acetoacetate ammonia versus glucose ammonia

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Transcription profiling of Rhizobium leguminosarum biovar viciae strain 3841 inoculated onto vetch seeds compared to cells grown in free-living culture on succinate ammonia AMS

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A GMC Oxidoreductase GmcA is required for symbiotic nitrogen fixation in Rhizobium leguminosarum bv. Viciae

Project description:GmcA is a FAD-containing enzyme belonging to the GMC (glucose-methanol-choline oxidase) family of oxidoreductases. A mutation in the R. leguminosarum gmcA gene was generated by homologous recombination. The mutation in gmcA did not affect the growth of R. leguminosarum, but it displayed decreased antioxidative capacity at H2O2 conditions higher than 5 mM. The gmcA mutant strain displayed no difference of glutathione reductase activity, but significantly lower level of the glutathione peroxidase activity than the wild type. Although the gmcA mutant can induce the formation of nodules, the symbiotic ability was severely impaired, which led to an abnormal nodulation phenotype coupled to a 30% reduction in the nitrogen fixation capacity. The observation on ultrastructure of 4-week pea nodules showed that the mutant bacteroids tended to start senescence earlier, and accumulate poly-β-hydroxybutyrate (PHB) granules. In addition, the gmcA mutant was severely impaired in rhizosphere colonization. Real-time quantitative PCR showed that the gmcA gene expression is significantly upregulated in all the detected stages of nodule development, and statistically significant decreases in the expression of the redoxin genes katG, katE and ohrB, were found in gmcA mutant bacteroids. LC-MS/MS analysis quantitative proteomics techniques were employed to compare differential gmcA mutant root bacteroids in response to the wild type infection. Sixty differentially expressed proteins were identified including 33 up-regulated and 27 down-regulated proteins. By sorting the identified proteins according to metabolic function, fifteen proteins were transporter protein, twelve proteins were related to stress response and virulence, and nine proteins were related to transcription factor activity. Moreover, nine proteins related to amino acid metabolism were over-expressed.

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