Open AccessInvolvement of the catalytically important Asp54 residue of Mycobacterium smegmatis DevR in protein–protein interactions between DevR and DevS
Author(s) -
Lee HaNa,
Lee NaOn,
Ko InJeong,
Kim Si Wouk,
Kang Beom Sik,
Oh JeongIl
Publication year - 2013
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12122
Subject(s) - mycobacterium smegmatis , response regulator , devs , histidine kinase , mutant , protein–protein interaction , regulator , phosphorylation , signal transducing adaptor protein , autophosphorylation , chemistry , microbiology and biotechnology , biology , biophysics , protein kinase a , biochemistry , computer science , gene , mycobacterium tuberculosis , modeling and simulation , medicine , tuberculosis , pathology , simulation
The Dev SR two‐component system in Mycobacterium smegmatis consists of the DevS histidine kinase and the DevR response regulator. It is a regulatory system that is involved in the adaptation of mycobacteria to hypoxic and NO stresses. Using the yeast two‐hybrid assay and pull‐down assay, it was demonstrated that the phosphoaccepting Asp (Asp54) of DevR is important for protein–protein interactions between DevR and DevS. The negative charge of Asp54 of DevR was shown to play an important role in protein–protein interactions between DevR and DevS. When the Lys104 residue, which is involved in transmission of conformational changes induced by phosphorylation of the response regulator, was replaced with Ala, the mutant form of DevR was not phosphorylated by DevS and functionally inactive in vivo . However, the K104A mutation in DevR only slightly affected protein–protein interactions between DevR and DevS.