From signal perception to signal transduction: ligand-induced dimeric switch of DctB sensory domain in solution.

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 Microbiol

journal_title

Molecular microbiology

authors

Nan B,Liu X,Zhou Y,Liu J,Zhang L,Wen J,Zhang X,Su XD,Wang YP

doi

10.1111/j.1365-2958.2010.07069.x

subject

Has Abstract

pub_date

2010-03-01 00:00:00

pages

1484-94

issue

6

eissn

0950-382X

issn

1365-2958

pii

MMI7069

journal_volume

75

pub_type

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