Proteomic Analysis of Rhizobium favelukesii LPU83 in Response to Acid Stress
Acid soils constitute a severe problem for leguminous crops mainly through a disturbance in rhizobium–legume interactions. Rhizobium favelukesiian acid-tolerant rhizobium able to nodulate alfalfais highly competitive for nodule occupation under acid conditions but inefficient for biologic nitrogen...
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Veröffentlicht in: | Journal of proteome research 2019-10, Vol.18 (10), p.3615-3629 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Acid soils constitute a severe problem for leguminous crops mainly through a disturbance in rhizobium–legume interactions. Rhizobium favelukesiian acid-tolerant rhizobium able to nodulate alfalfais highly competitive for nodule occupation under acid conditions but inefficient for biologic nitrogen fixation. In this work, we obtained a general description of the acid-stress response of R. favelukesii LPU83 by means of proteomics by comparing the total proteome profiles in the presence or absence of acid stress by nanoflow ultrahigh-performance liquid chromatography coupled to mass spectrometry. Thus, a total of 336 proteins were identified with a significant differential expression, 136 of which species were significantly overexpressed and 200 underexpressed in acidity. An in silico functional characterization with those respective proteins revealed a complex and pleiotropic response by these rhizobia involving components of oxidative phosphorylation, glutamate metabolism, and peptidoglycan biosynthesis, among other pathways. Furthermore, a lower permeability was evidenced in the acid-stressed cells along with several overexpressed proteins related to γ-aminobutyric acid metabolism, such as the gene product of livK, which gene was mutated. This mutant exhibited an acid-sensitive phenotype in agreement with the proteomics results. We conclude that both the γ-aminobutyric acid metabolism and a modified cellular envelope could be relevant to acid tolerance in R. favelukesii. |
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ISSN: | 1535-3893 1535-3907 |
DOI: | 10.1021/acs.jproteome.9b00275 |