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Title 

Mechanism of the pH-induced conformational change in the sensor domain of the DraK histidine kinase via the E83, E105, and E107 residues

Authors 

K J YeoYoung-Soo HongJ G JeeJae Kyoung LeeHyo Jeong KimJ W ParkE H KimE HwangSang Yoon KimEun Gyeong LeeOh Suk KwonH K Cheong

Publisher 

Public Library of Science

Issue Date 

2014

Citation 

Plos One, vol. 9, no. 9, pp. e107168-e107168

Abstract 

The DraR/DraK two-component system was found to be involved in the differential regulation of antibiotic biosynthesis in a medium-dependent manner; however, its function and signaling and sensing mechanisms remain unclear. Here, we describe the solution structure of the extracellular sensor domain of DraK and suggest a mechanism for the pH-dependent conformational change of the protein. The structure contains a mixed alpha-beta fold, adopting a fold similar to the ubiquitous sensor domain of histidine kinase. A biophysical study demonstrates that the E83, E105, and E107 residues have abnormally high pKa values and that they drive the pH-dependent conformational change for the extracellular sensor domain of DraK. We found that a triple mutant (E83L/E105L/E107A) is pH independent and mimics the low pH structure. An in vivo study showed that DraK is essential for the recovery of the pH of Streptomyces coelicolor growth medium after acid shock. Our findings suggest that the DraR/DraK two-component system plays an important role in the pH regulation of S. coelicolor growth medium. This study provides a foundation for the regulation and the production of secondary metabolites in Streptomyces.

ISSN 

1932-6203

Link 

http://dx.doi.org/10.1371/journal.pone.0107168

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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