High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila

High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila

Legionella pneumophila RpoS (LpRpoS), an alternative sigma factor of RNA polymerase (RNAP), is essential for virulence and stress resistance. To investigate the mechanism of RpoS in the intracellular pathogen L. pneumophila, we determined the high-resolution crystal structure of the LpRpoS 95–195 co...

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Bibliographic Details
Main Authors: Nannan Zhang, Xiaofang Chen, Xiaojian Gong, Tao Li, Zhiyuan Xie, Muhammad Fazal Hameed, Mingzhu Wang, Honghua Ge
Format: Article
Language:English
Published: MDPI AG 2018-01-01
Series:Crystals
Subjects:
RpoS
crystal structure
Legionella pneumophila
intracellular pathogen
regulatory factor
Online Access:http://www.mdpi.com/2073-4352/8/2/54
Description
Summary:Legionella pneumophila RpoS (LpRpoS), an alternative sigma factor of RNA polymerase (RNAP), is essential for virulence and stress resistance. To investigate the mechanism of RpoS in the intracellular pathogen L. pneumophila, we determined the high-resolution crystal structure of the LpRpoS 95–195 containing a partial region 1.2 and region 2. The structure of LpRpoS 95–195 reveals that the conserved residues are critical for promoter melting, DNA and core RNAP binding. The differences in regulatory factor binding site between Escherichia coli RpoS and LpRpoS suggest that LpRpoS may employ a distinct mechanism to recruit alternative regulatory factors controlling transcription initiation.
ISSN:2073-4352

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