scholarly journals The Crystal Structure of the Transcriptional Regulator HucR from Deinococcus radiodurans Reveals a Repressor Preconfigured for DNA Binding

2006 ◽  
Vol 360 (1) ◽  
pp. 168-177 ◽  
Author(s):  
Tee Bordelon ◽  
Steven P. Wilkinson ◽  
Anne Grove ◽  
Marcia E. Newcomer
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Deinococcus Radiodurans ◽  
Transcriptional Regulator

scholarly journals Crystal structure and DNA-binding analysis of RecO from Deinococcus radiodurans

2005 ◽  
Vol 24 (5) ◽  
pp. 906-918 ◽  
Author(s):  
Ingar Leiros ◽  
Joanna Timmins ◽  
David R Hall ◽  
Sean McSweeney
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Deinococcus Radiodurans ◽  
Binding Analysis

scholarly journals Structural basis of hypoxic gene regulation by the Rv0081 transcription factor ofMycobacterium tuberculosis

2018 ◽  
Author(s):  
Ashwani Kumar ◽  
Swastik Phulera ◽  
Arshad Rizvi ◽  
Parshuram Sonawane ◽  
Hemendra Singh Panwar ◽  
...  
Keyword(s):  
Gene Expression ◽  
Crystal Structure ◽  
Gene Regulation ◽  
Transcription Factor ◽  
Dna Binding ◽  
Metal Binding ◽  
Transcriptional Regulator ◽  
Tuberculosis Infection ◽  
Structural Basis ◽  
Latent Phase

ABSTRACTThe transcription factor Rv0081 ofM. tuberculosiscontrols the hypoxic gene expression and acts as a regulatory hub in the latent phase of tuberculosis infection. We report here the crystal structure of Rv0081 at 3.3 Å resolution revealing that it belongs to the well-known ArsR/SmtB family proteins. ArsR/SmtB family transcriptional repressors exert gene regulation by reversible metal binding. Hypoxia in general is sensed by bacterial transcriptional regulators via metals or Cys-mediated thiol switches. Oxygen sensing typically leads to transcriptional repressor changing its conformational state with altered DNA-binding property under different oxygen levels. Surprisingly Rv0081 neither has a metal binding domain nor does it possess Cys residues suggesting an alternate mechanism of gene regulation. Our structural analysis identified Ser 48, Ser 49, Ser 52 and Gln 53 as potential residues of Rv0081 involved in DNA binding. We probed DNA-binding of Rv0081 with electrophoretic mobility shift assay (EMSA) as well as surface plasmon resonance (SPR), where the Alanine mutants of these residues showed diminished DNA binding. Similarly, Aspartate mutants of these Ser residues was shown to fail to bind to DNA. Since, phosphorylation of various regulatory proteins is one of the important controlling mechanisms, we expected the role of Ser-phosphorylation of Rv0081 in hypoxic condition. Probing Rv0081 with anti-phosphoserine antibodies inM. tuberculosiscell lysate showed marked enhancement in the phosphorylation of Rv0081 protein under hypoxia. Overall, our structural and biochemical analysis provides the molecular basis for the regulation of Rv0081 in the latent phase of tuberculosis infection.IMPORTANCETuberculosis is one of the deadliest infectious diseases caused by the bacteriumMycobacterium tuberculosis. In about 90% of the infected people,M. tuberculosisexists in a dormant or a latent stage which can be reactivated in favorable conditions. Hypoxia (low oxygen pressure) is one of causes of dormancy. Understanding hypoxic gene regulation inM. tuberculosisis therefore an important step to understand latency. Rv0081 is a transcriptional regulator of genes expressed during hypoxia. In order to understand the mechanism by which Rv00081 regulates gene expression during hypoxia, we have solved the crystal structure of Rv0081 and identified amino acid residues which are critical in its transcriptional regulator activity. The crystal structure is suggestive of mechanism of gene regulation under hypoxia.

scholarly journals Crystal Structure of the DNA-binding Domain of the LysR-type Transcriptional Regulator CbnR in Complex with a DNA Fragment of the Recognition-binding Site

2018 ◽  
Vol 60 (2-3) ◽  
pp. 135-141
Author(s):  
Miki SENDA ◽  
Naruhiko ADACHI ◽  
Toshiya SENDA ◽  
Maharani Pertiwi KOENTJORO ◽  
Naoto OGAWA
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Binding Site ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Dna Fragment

scholarly journals Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric states

2013 ◽  
Vol 41 (21) ◽  
pp. 9934-9944 ◽  
Author(s):  
Seiji N. Sugiman-Marangos ◽  
John K. Peel ◽  
Yoni M. Weiss ◽  
Rodolfo Ghirlando ◽  
Murray S. Junop
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Deinococcus Radiodurans ◽  
Higher Order ◽  
Binding Surface

Letter to Editor: Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric β-barrel fold

2004 ◽  
Vol 30 (2) ◽  
pp. 211-214 ◽  
Author(s):  
Alejandro D. Nadra ◽  
Tommaso Eliseo ◽  
Yu-Keung Mok ◽  
Fabio C.L. Almeida ◽  
Mark Bycroft ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hpv 16

scholarly journals Crystal Structure ofDeinococcus radioduransRecQ Helicase Catalytic Core Domain: The Interdomain Flexibility

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Sheng-Chia Chen ◽  
Chi-Hung Huang ◽  
Chia Shin Yang ◽  
Tzong-Der Way ◽  
Ming-Chung Chang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Deinococcus Radiodurans ◽  
Domain Architecture ◽  
Genome Integrity ◽  
Catalytic Core Domain ◽  
Catalytic Core ◽  
Core Domain ◽  
Winged Helix ◽  
Dna Helicases ◽  
E Coli

RecQ DNA helicases are key enzymes in the maintenance of genome integrity, and they have functions in DNA replication, recombination, and repair. In contrast to most RecQs, RecQ fromDeinococcus radiodurans(DrRecQ) possesses an unusual domain architecture that is crucial for its remarkable ability to repair DNA. Here, we determined the crystal structures of the DrRecQ helicase catalytic core and its ADP-bound form, revealing interdomain flexibility in its first RecA-like and winged-helix (WH) domains. Additionally, the WH domain of DrRecQ is positioned in a different orientation from that of theE. coliRecQ (EcRecQ). These results suggest that the orientation of the protein during DNA-binding is significantly different when comparing DrRecQ and EcRecQ.

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