Abstract:
:Sinorhizobium meliloti DctB is a typical transmembrane sensory histidine kinase, which senses C(4)-dicarboxylic acids (DCA) and regulates the expression of DctA, the DCA transporter. We previously reported the crystal structures of its periplasmic sensory domain (DctBp) in apo and succinate-bound states, and these structures showed dramatic conformational changes at dimeric level. Here we show a ligand-induced dimeric switch in solution and a strong correlation between DctBp's dimerization states and the in vivo activities of DctB. Using site-directed mutagenesis, we identify important determinants for signal perception and transduction. Specifically, we show that the ligand-binding pocket is essential for DCA-induced 'on' activity of DctB. Mutations at different sections of DctBp's dimerization interface can lock full-length DctB at either 'on' or 'off' state, independent of ligand binding. Taken together, these results suggest that DctBp's signal perception and transduction occur through a 'ligand-induced dimeric switch', in which the changes in the dimeric conformations upon ligand binding are responsible for the signal transduction in DctB.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Nan B,Liu X,Zhou Y,Liu J,Zhang L,Wen J,Zhang X,Su XD,Wang YPdoi
10.1111/j.1365-2958.2010.07069.xsubject
Has Abstractpub_date
2010-03-01 00:00:00pages
1484-94issue
6eissn
0950-382Xissn
1365-2958pii
MMI7069journal_volume
75pub_type
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