4.6 Article

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

Journal

CRYSTALS
Volume 8, Issue 2, Pages -

Publisher

MDPI
DOI: 10.3390/cryst8020054

Keywords

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

Funding

  1. Science Foundation of Anhui University [KYXL2016105, J18520219]
  2. National Natural Science Foundation of China [31400641, 31270770]

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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.

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