A Novel Tetrameric Assembly Configuration in VV2_1132, a LysR-Type Transcriptional Regulator in Vibrio vulnificus
Yongdae Jang1, Garam Choi1,2, Seokho Hong1, Inseong Jo1, Jinsook Ahn1, Sang Ho Choi1,2,*, and Nam-Chul Ha1,*
1Research Institute for Agriculture and Life Sciences, Center for Food and Bioconvergence, Center for Food Safety and Toxicology, Seoul National University, Seoul 08826, Korea, 2National Research Laboratory of Molecular Microbiology and Toxicology, Seoul National University, Seoul 08826, Korea
*Correspondence: choish@snu.ac.kr (SHC); hanc210@snu.ac.kr (NCH)
Received September 4, 2017; Revised November 3, 2017; Accepted January 8, 2018.; Published online February 27, 2018.
© Korean Society for Molecular and Cellular Biology. All rights reserved.

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LysR-type transcriptional regulators (LTTRs) contain an Nterminal DNA binding domain (DBD) and a C-terminal regulatory domain (RD). Typically, LTTRs function as homotetramers. VV2_1132 was identified in Vibrio vulnificus as an LTTR that is a homologue of HypT (also known as YjiE or QseD) in Escherichia coli. In this study, we determined the crystal structure of full-length VV2_1132 at a resolution of 2.2 Å, thereby revealing a novel combination of the domains in the tetrameric assembly. Only one DBD dimer in the tetramer can bind to DNA, because the DNA binding motifs of the other DBD dimer are completely buried in the tetrameric assembly. Structural and functional analyses of VV2_1132 suggest that it might not perform the same role as E. coli HypT, indicating that further study is required to elucidate the function of this gene in V. vulnificus. The unique structure of VV2_1132 extends our knowledge of LTTR function and mechanisms of action.  
Keywords: LysR type transcriptional regulator, Vibrio vulnificus, X-ray crystallography

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28 February 2018 Volume 41,
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