Journal article
Sinorhizobium meliloti flavin secretion and bacteria-host interaction: role of the bifunctional RibBA protein
Molecular plant-microbe interactions, Vol.27(5), pp.437-445
05/2014
Handle:
https://hdl.handle.net/2376/107399
PMID: 24405035
Abstract
Sinorhizobium meliloti, the nitrogen-fixing bacterial symbiont of Medicago spp. and other legumes, secretes a considerable amount of riboflavin. This precursor of the cofactors flavin mononucleotide and flavin adenine dinucleotide is a bioactive molecule that has a beneficial effect on plant growth. The ribBA gene of S. meliloti codes for a putative bifunctional enzyme with dihydroxybutanone phosphate synthase and guanosine triphosphate (GTP) cyclohydrolase II activities, catalyzing the initial steps of the riboflavin biosynthesis pathway. We show here that an in-frame deletion of ribBA does not cause riboflavin auxotrophy or affect the ability of S. meliloti to establish an effective symbiosis with the host plant but does affect the ability of the bacteria to secrete flavins, colonize host-plant roots, and compete for nodulation. A strain missing the RibBA protein retains considerable GTP cyclohydrolase II activity. Based on these results, we hypothesize that S. meliloti has two partly interchangeable modules for biosynthesis of riboflavin, one fulfilling the internal need for flavins in bacterial metabolism and the other producing riboflavin for secretion. Our data also indicate that bacteria-derived flavins play a role in communication between rhizobia and the legume host and that the RibBA protein is important in this communication process even though it is not essential for riboflavin biosynthesis and symbiosis.
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Details
- Title
- Sinorhizobium meliloti flavin secretion and bacteria-host interaction: role of the bifunctional RibBA protein
- Creators
- Svetlana N YurgelJennifer RiceElizabeth DomreisJoseph LynchNa SaZeeshan QamarSathish RajamaniMengsheng GaoSanja RojeWolfgang D Bauer
- Publication Details
- Molecular plant-microbe interactions, Vol.27(5), pp.437-445
- Academic Unit
- Biological Chemistry, Institute of
- Publisher
- United States
- Identifiers
- 99900547400401842
- Language
- English
- Resource Type
- Journal article