Sinorhizobium meliloti YrbA binds divalent metal cations using two conserved histidines
Thomas Roret1,2, Geneviève Alloing3, Jean-Michel Girardet1
1Université de Lorraine, INRAE, IAM, Nancy, France.
Bioscience Reports
|September 24, 2020
Summary
Sinorhizobium meliloti
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Sinorhizobium meliloti forms symbiotic nodules with legumes.
- The roles of BolA-like proteins (BolA and YrbA) in S. meliloti are unknown.
- BolA proteins and glutaredoxins (Grxs) often regulate iron homeostasis and iron-sulfur (Fe-S) protein maturation.
Purpose of the Study:
- To investigate the structure-function relationship of SmYrbA.
- To determine the role of SmYrbA in metal ion coordination and heterodimer formation.
- To elucidate the function of BolA-like proteins in S. meliloti iron homeostasis and symbiosis.
Main Methods:
- Structure-function analysis of SmYrbA.
- Metal ion coordination assays.
- Heterodimerization studies with SmGrx2.
- Analysis of metal tolerance in S. meliloti mutant strains.
- Assessment of nodulation phenotypes in Medicago truncatula.
Main Results:
- SmYrbA coordinates various divalent metal ions (Fe2+, Co2+, Ni2+, Cu2+, Zn2+) via His32 and His67 residues.
- SmYrbA forms heterodimers with SmGrx2.
- YrbA is involved in regulating iron homeostasis in S. meliloti.
- The yrbA bolA mutant shows mild nodulation defects, distinct from grx2 mutant phenotypes.
Conclusions:
- SmYrbA plays a role in metal ion binding and potentially Fe-S cluster coordination.
- YrbA contributes to iron homeostasis regulation in S. meliloti.
- BolA-like proteins have functions in bacterial symbiosis that may be independent of SmGrx2.
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