Crystal Structures of SlyA Protein, a Master Virulence Regulator of Salmonella, in Free and DNA-bound States

Journal Article · Thu Nov 17 04:00:00 EST 2011 · J. Biol. Chem.

DOI:https://doi.org/10.1074/jbc.M111.245258· OSTI ID:1021775

Dolan, Kyle T; Duguid, Erica M; He, Chuan ^[1]

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1. UC

SlyA is a master virulence regulator that controls the transcription of numerous genes in Salmonella enterica. We present here crystal structures of SlyA by itself and bound to a high-affinity DNA operator sequence in the slyA gene. SlyA interacts with DNA through direct recognition of a guanine base by Arg-65, as well as interactions between conserved Arg-86 and the minor groove and a large network of non-base-specific contacts with the sugar phosphate backbone. Our structures, together with an unpublished structure of SlyA bound to the small molecule effector salicylate (Protein Data Bank code 3DEU), reveal that, unlike many other MarR family proteins, SlyA dissociates from DNA without large conformational changes when bound to this effector. We propose that SlyA and other MarR global regulators rely more on indirect readout of DNA sequence to exert control over many genes, in contrast to proteins (such as OhrR) that recognize a single operator.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: OTHERNIH
• OSTI ID: 1021775
• Journal Information: J. Biol. Chem., Journal Name: J. Biol. Chem. Journal Issue: (25) ; 06, 2011 Vol. 286; ISSN JBCHA3; ISSN 0021-9258
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
CONFORMATIONAL CHANGES
CRYSTAL STRUCTURE
CRYSTALLOGRAPHY
DNA
GENES
GUANINE
PHOSPHATES
PROTEINS
REGULATIONS
SACCHAROSE
SALMONELLA
TRANSCRIPTION
TRANSCRIPTION FACTORS
VIRULENCE