AI Article Synopsis
- The SorC/DeoR family is a group of bacteria proteins that help control how bacteria use sugar and communicate with each other.
- Scientists studied two specific proteins, bsDeoR and bsCggR, from a type of bacteria called Bacillus subtilis to understand how they connect to DNA.
- They found detailed structures of these proteins when they attach to DNA and discovered they might work in a similar way to other proteins in their family when recognizing DNA.
Article Abstract
The SorC/DeoR family is a large family of bacterial transcription regulators that are involved in the control of carbohydrate metabolism and quorum sensing. To understand the structural basis of DNA recognition, structural studies of two functionally characterized SorC/DeoR family members from Bacillus subtilis were performed: the deoxyribonucleoside regulator bsDeoR and the central glycolytic genes regulator bsCggR. Each selected protein represents one of the subgroups that are recognized within the family. Crystal structures were determined of the N-terminal DNA-binding domains of bsDeoR and bsCggR in complex with DNA duplexes representing the minimal operator sequence at resolutions of 2.3 and 2.1 Å, respectively. While bsDeoR contains a homeodomain-like HTH-type domain, bsCggR contains a winged helix-turn-helix-type motif. Both proteins form C2-symmetric dimers that recognize two consecutive major grooves, and the protein-DNA interactions have been analyzed in detail. The crystal structures were used to model the interactions of the proteins with the full DNA operators, and a common mode of DNA recognition is proposed that is most likely to be shared by other members of the SorC/DeoR family.
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Structure and function of bacterial transcription regulators of the SorC family.
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September 2024
Structural Biology, Institute of Organic Chemistry and Biochemistry of Czech Academy of Sciences, Prague, Czechia.
The SorC family is a large group of bacterial transcription regulators involved in controlling carbohydrate catabolism and quorum sensing. SorC proteins consist of a conserved C-terminal effector-binding domain and an N-terminal DNA-binding domain, whose type divides the family into two subfamilies: SorC/DeoR and SorC/CggR. Proteins of the SorC/CggR subfamily are known to regulate the key node of glycolysis-triose phosphate interconversion.
View Article and Find Full Text PDFStructural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family.
Acta Crystallogr D Struct Biol
November 2021
Structural Biology, Institute of Organic Chemistry and Biochemistry of Czech Academy of Sciences, Flemingovo nám. 2, 166 10 Prague, Czech Republic.
Article Synopsis
- The SorC/DeoR family is a group of bacteria proteins that help control how bacteria use sugar and communicate with each other.
- Scientists studied two specific proteins, bsDeoR and bsCggR, from a type of bacteria called Bacillus subtilis to understand how they connect to DNA.
- They found detailed structures of these proteins when they attach to DNA and discovered they might work in a similar way to other proteins in their family when recognizing DNA.
Genome-wide transcriptome analysis of the adaptive response of Enterococcus faecalis to copper exposure.
Biometals
December 2010
Laboratorio de Bioinformática y Expresión Génica, INTA, Universidad de Chile, El Libano 5524, Macul, Santiago, Chile.
In this work we investigated the adaptive response of E. faecalis to Cu and the role of CopY, a Cu-dependent repressor, in the regulation of Cu metabolism. In doing so, we examined the whole-genome transcriptional response of E.
View Article and Find Full Text PDFCrystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates.
Mol Microbiol
August 2008
Department of Biochemistry, The University of Texas Southwestern Medical Center at Dallas, Dallas, TX, USA.
Expression of genes in the gapA operon encoding five enzymes for triose phosphate interconversion in Bacillus subtilis is negatively regulated by the Central glycolytic genes Regulator (CggR). CggR belongs to the large SorC/DeoR family of prokaryotic transcriptional regulators, characterized by an N-terminal DNA-binding domain and a large C-terminal effector-binding domain. When no glucose is present in growth media, CggR binds to its target DNA sequence and blocks the transcription of genes in the gapA operon.
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