Preprint Article Version 1 This version not peer reviewed

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

Version 1 : Received: 25 November 2017 / Approved: 29 November 2017 / Online: 29 November 2017 (05:04:33 CET)

A peer-reviewed article of this Preprint also exists.

Zhang, N.; Chen, X.; Gong, X.; Li, T.; Xie, Z.; Hameed, M.F.; Wang, M.; Ge, H. High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila. Crystals 2018, 8, 54. Zhang, N.; Chen, X.; Gong, X.; Li, T.; Xie, Z.; Hameed, M.F.; Wang, M.; Ge, H. High-Resolution Crystal Structure of RpoS Fragment including a Partial Region 1.2 and Region 2 from the Intracellular Pathogen Legionella pneumophila. Crystals 2018, 8, 54.

Journal reference: Crystals 2018, 8, 54
DOI: 10.3390/cryst8020054

Abstract

Legionella pneumophila RpoS (LpRpoS) is an alternative sigma factor of RNA polymerase (RNAP) 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 (residues 95-194) containing a partial region 1.2 and region 2. The structure of LpRpoS (residues 95-194) 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.

Subject Areas

RpoS; crystal structure; Legionella pneumophila; intracellular pathogen; regulatory factor

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