Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family

0548549 - ÚMG 2022 RIV GB eng J - Journal Article
Šoltysová, M. - Sieglová, Irena - Fábry, Milan - Brynda, Jiří - Škerlová, Jana - Řezáčová, Pavlína
Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family.
Acta Crystallographica Section D-Structural Biology. Roč. 77, č. 11 (2021), s. 1411-1424. ISSN 2059-7983. E-ISSN 2059-7983
Institutional support: RVO:68378050
Keywords : SorC/DeoR family * protein-DNA complexes * transcription repressors * Bacillus subtilis * deoxyribonucleoside regulator bsDeoR * gene regulator bsCggR * carbohydrate catabolism
OECD category: Biochemistry and molecular biology
Impact factor: 5.699, year: 2021
Method of publishing: Limited access
https://scripts.iucr.org/cgi-bin/paper?S2059798321009633

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 degrees representing the minimal operator sequence at resolutions of 2.3 and 2.1 angstrom, respectively. While bsDeoR(DBD) contains a homeodomain-like HTH-type domain, bsCggR(DBD) 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.
Permanent Link: http://hdl.handle.net/11104/0324596