scholarly journals Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB fromEscherichia coli

2016 ◽  
Vol 25 (12) ◽  
pp. 2216-2224 ◽  
Author(s):  
Ekaterina V. Filippova ◽  
Zdzislaw Wawrzak ◽  
Jiapeng Ruan ◽  
Sergii Pshenychnyi ◽  
Richard M. Schultz ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Stress Response ◽  
Response Regulator ◽  
Fromescherichia Coli ◽  
Receiver Domain

scholarly journals Phospho-dependent Signaling during the General Stress Response by the Atypical Response Regulator and ClpXP Adaptor RssB

2021 ◽  
Author(s):  
Jacob Schwartz ◽  
Jonghyeon Son ◽  
Christiane Brugger ◽  
Alexandra M. Deaconescu
Keyword(s):  
Stress Response ◽  
Response Regulator ◽  
Model Organism ◽  
Coupling Scheme ◽  
Response Regulators ◽  
General Stress Response ◽  
Signaling Model ◽  
Receiver Domain ◽  
General Stress ◽  
Promoter Specificity

ABSTRACTIn the model organism Escherichia coli and related species, the general stress response relies on tight regulation of the intracellular levels of the promoter specificity subunit RpoS. RpoS turnover is exclusively dependent on RssB, a two-domain response regulator that functions as an adaptor that delivers RpoS to ClpXP for proteolysis. Here we report crystal structures of the receiver domain of RssB both in its unphosphorylated form and bound to the phosphomimic BeF3−. Surprisingly, we find only modest differences between these two structures, suggesting that truncating RssB may partially activate the receiver domain to a “meta-active” state. Our structural and sequence analysis points to RssB proteins not conforming to either the Y-T coupling scheme for signaling seen in prototypical response regulators, such as CheY, or to the signaling model of the less understood FATGUY proteins.

scholarly journals Crystal Structure of the CheA Histidine Phosphotransfer Domain that Mediates Response Regulator Phosphorylation in Bacterial Chemotaxis

2001 ◽  
Vol 276 (33) ◽  
pp. 31074-31082 ◽  
Author(s):  
Lionel Mourey ◽  
Sandra Da Re ◽  
Jean-Denis Pédelacq ◽  
Tatiana Tolstykh ◽  
Cécile Faurie ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Response Regulator ◽  
Bacterial Chemotaxis ◽  
Histidine Phosphotransfer

scholarly journals Deciphering the activation and recognition mechanisms of Staphylococcus aureus response regulator ArlR

2019 ◽  
Vol 47 (21) ◽  
pp. 11418-11429 ◽  
Author(s):  
Zhenlin Ouyang ◽  
Fang Zheng ◽  
Jared Y Chew ◽  
Yingmei Pei ◽  
Jinhong Zhou ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Dna Binding ◽  
Crystal Structures ◽  
Response Regulator ◽  
Regulatory System ◽  
Repeat Sequence ◽  
Effector Domain ◽  
Receiver Domain ◽  
Regulation Mechanisms ◽  
Significant Conformational Change

Abstract Staphylococcus aureus ArlRS is a key two-component regulatory system necessary for adhesion, biofilm formation, and virulence. The response regulator ArlR consists of a C-terminal DNA-binding effector domain and an N-terminal receiver domain that is phosphorylated by ArlS, the cognate transmembrane sensor histidine kinase. We demonstrate that the receiver domain of ArlR adopts the canonical α5β5 response regulator assembly, which dimerizes upon activation, using beryllium trifluoride as an aspartate phosphorylation mimic. Activated ArlR recognizes a 20-bp imperfect inverted repeat sequence in the ica operon, which is involved in intercellular adhesion polysaccharide production. Crystal structures of the inactive and activated forms reveal that activation induces a significant conformational change in the β4-α4 and β5-α5-connecting loops, in which the α4 and α5 helices constitute the homodimerization interface. Crystal structures of the DNA-binding ArlR effector domain indicate that it is able to dimerize via a non-canonical β1–β2 hairpin domain swapping, raising the possibility of a new mechanism for signal transduction from the receiver domain to effector domain. Taken together, the current study provides structural insights into the activation of ArlR and its recognition, adding to the diversity of response regulation mechanisms that may inspire novel antimicrobial strategies specifically targeting Staphylococcus.

scholarly journals Regulation of Oxidative Stress Response by CosR, an Essential Response Regulator in Campylobacter jejuni

PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e22300 ◽  
Author(s):  
Sunyoung Hwang ◽  
Minkyeong Kim ◽  
Sangryeol Ryu ◽  
Byeonghwa Jeon
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Campylobacter Jejuni ◽  
Response Regulator ◽  
Oxidative Stress Response
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