Document Detail


Nitrogen metabolism in S. meliloti?alfalfa symbiosis: Dissecting the role of GlnD and PII proteins.
MedLine Citation:
PMID:  22074345     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
To contribute nitrogen for plant growth and establish an effective symbiosis with alfalfa, S. meliloti Rm1021 needs normal operation of the GlnD protein, a bifunctional uridylyltransferase/uridylyl-cleavage enzyme that measures cellular nitrogen status and initiates a nitrogen stress response (NSR) (Yurgel and Kahn, 2008). However, the only two known targets of GlnD modification in Rm1021, the PII proteins GlnB and GlnK, are not necessary for effectiveness (Yurgel et al. 2010). We introduced a Tyr-Phe variant of GlnB, which cannot be uridylylated, into a glnBglnK background to approximate the expected state in a glnD-sm2 mutant and this strain was effective. These results suggested that unmodified PII does not inhibit effectiveness. We also generated a glnBglnKglnD triple mutant and used this and other mutants to dissect the role of these proteins in regulating the free-living NSR and nitrogen metabolism in symbiosis. The glnD-sm2 mutation was dominant to the glnBglnK mutations in symbiosis but recessive in some free-living phenotypes. The data show that the GlnD protein has a role in free-living growth and in symbiotic nitrogen exchange that does not depend on the PII proteins, suggesting that S. meliloti GlnD can communicate with the cell by alternate mechanisms.
Authors:
Svetlana N Yurgel; Jennifer Rice; Michael Kahn
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-10
Journal Detail:
Title:  Molecular plant-microbe interactions : MPMI     Volume:  -     ISSN:  0894-0282     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9107902     Medline TA:  Mol Plant Microbe Interact     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Washington State University , Institute of Biological Chemistry , Pullman, WA, 99164-6340 , Pullman, Washington, United States, 99164-6340 ; syurgel@wsu.edu.
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