PXD017835 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Antioxidant mechanism of glutaredoxins and their role in symbiotic nitrogen fixation in Rhizobium leguminosarum bv. viciae 3841 |
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. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:16:05.052.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Guojun Cheng |
SpeciesList | scientific name: Rhizobium leguminosarum bv. viciae; NCBI TaxID: 387; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-03-02 23:35:47 | ID requested | |
1 | 2020-12-01 23:25:02 | announced | |
⏵ 2 | 2024-10-22 05:16:05 | announced | 2024-10-22: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Glutaredoxins |
Rhizobium leguminosarum bv. viciae 3841 |
antioxidant capacity |
symbiotic nitrogen fixation |
Proteomics analysis |
Contact List
Guojun Cheng |
contact affiliation | College of Life Sciences, South-Central University for Nationalities |
contact email | chengguojun@mail.scuec.edu.cn |
lab head | |
Guojun Cheng |
contact affiliation | College of Life Sciences, South-Central University for Nationalities |
contact email | chengguojun@mail.scuec.edu.cn |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/12/PXD017835 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD017835
- Label: PRIDE project
- Name: Antioxidant mechanism of glutaredoxins and their role in symbiotic nitrogen fixation in Rhizobium leguminosarum bv. viciae 3841