X-ray crystal structure of putative transcription regulator lmo2088 from Listeria monocytogenes

Abdus Samad; Yuelong Li; Caiying Zhang; Feng Chen; Weihong Zeng; Xiaojiao Fan; Tengchuan Jin

doi:10.1016/j.bbrc.2019.10.033

X-ray crystal structure of putative transcription regulator lmo2088 from Listeria monocytogenes

Biochem Biophys Res Commun. 2019 Dec 3;520(2):434-440. doi: 10.1016/j.bbrc.2019.10.033. Epub 2019 Oct 10.

Authors

Abdus Samad¹, Yuelong Li², Caiying Zhang², Feng Chen², Weihong Zeng², Xiaojiao Fan², Tengchuan Jin³

Affiliations

¹ Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China; Division of Molecular Medicine, Hefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China.
² Division of Molecular Medicine, Hefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China.
³ Department of Obstetrics and Gynecology, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China; Division of Molecular Medicine, Hefei National Laboratory for Physical Sciences at Microscale, CAS Key Laboratory of Innate Immunity and Chronic Disease, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China; CAS Center for Excellence in Molecular Cell Science, Shanghai, China. Electronic address: jint@ustc.edu.cn.

PMID: 31607473
DOI: 10.1016/j.bbrc.2019.10.033

Abstract

Listeria monocytogenes is a gram-positive food borne pathogen. The lmo2088 belongs to the TetR family of transcriptional regulators from L. monocytogenes. These transcriptional factors regulate multidrug resistance transporters in L. monocytogenes. Here, we report native protein crystal structure of lmo2088 at a resolution of 1.7 Å. Lmo2088 comprises of an N-terminal DNA binding domain and a variable C-terminal effector binding domain. Furthermore, we identified specific consensus sequences selected by systematic evolution of ligands by exponential enrichment in vitro. The specific binding of lmo2088 with DNA consensus sequence was validated by electrophoretic mobility shift assay, fluorescence polarization and isothermal titration calorimetry. We speculate that the structure of lmo2088 might provide an insight into the regulatory function of lmo2088 of L. monocytogenes.

Keywords: Consensus sequence; DNA binding; Helix-turn-helix; Listeria monocytogenes; Protein: DNA complex; TetR/AcrR; Transcription factor.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Binding Sites
Calorimetry
Crystallography, X-Ray
DNA / chemistry
DNA / metabolism
Electrophoretic Mobility Shift Assay
Fluorescence Polarization
Listeria monocytogenes / chemistry*
Listeria monocytogenes / genetics
Models, Molecular
Protein Conformation
Transcription Factors / chemistry
Transcription Factors / genetics
Transcription Factors / metabolism

Substances

Bacterial Proteins
Transcription Factors
DNA