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Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.
Chembazhi, Ullas Valiya; Patil, Vinod Vikas; Sah, Shivjee; Reeve, Wayne; Tiwari, Ravi P; Woo, Euijeon; Varshney, Umesh.
Afiliación
  • Chembazhi UV; Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
  • Patil VV; Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, 125 Gwahak-Ro, Yuseon-Gu, Daejeon 34141, Republic of Korea.
  • Sah S; Department of Bio-Analytical Science, University of Science and Technology, Daejeon 34113, Republic of Korea.
  • Reeve W; Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
  • Tiwari RP; Centre for Rhizobium Studies, School of Veterinary and Life Sciences, Murdoch University, Murdoch, WA 6150, Australia.
  • Woo E; Centre for Rhizobium Studies, School of Veterinary and Life Sciences, Murdoch University, Murdoch, WA 6150, Australia.
  • Varshney U; Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, 125 Gwahak-Ro, Yuseon-Gu, Daejeon 34141, Republic of Korea.
Nucleic Acids Res ; 45(10): 5863-5876, 2017 Jun 02.
Article en En | MEDLINE | ID: mdl-28369586
Repair of uracils in DNA is initiated by uracil DNA glycosylases (UDGs). Family 1 UDGs (Ung) are the most efficient and ubiquitous proteins having an exquisite specificity for uracils in DNA. Ung are characterized by motifs A (GQDPY) and B (HPSPLS) sequences. We report a novel dimeric UDG, Blr0248 (BdiUng) from Bradyrhizobium diazoefficiens. Although BdiUng contains the motif A (GQDPA), it has low sequence identity to known UDGs. BdiUng prefers single stranded DNA and excises uracil, 5-hydroxymethyl-uracil or xanthine from it. BdiUng is impervious to inhibition by AP DNA, and Ugi protein that specifically inhibits family 1 UDGs. Crystal structure of BdiUng shows similarity with the family 4 UDGs in its overall fold but with family 1 UDGs in key active site residues. However, instead of a classical motif B, BdiUng has a uniquely extended protrusion explaining the lack of Ugi inhibition. Structural and mutational analyses of BdiUng have revealed the basis for the accommodation of diverse substrates into its substrate binding pocket. Phylogenetically, BdiUng belongs to a new UDG family. Bradyrhizobium diazoefficiens presents a unique scenario where the presence of at least four families of UDGs may compensate for the absence of an efficient family 1 homologue.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Uracilo / ADN Bacteriano / Bradyrhizobium / Reparación del ADN / Uracil-ADN Glicosidasa Idioma: En Revista: Nucleic Acids Res Año: 2017 Tipo del documento: Article País de afiliación: India Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Uracilo / ADN Bacteriano / Bradyrhizobium / Reparación del ADN / Uracil-ADN Glicosidasa Idioma: En Revista: Nucleic Acids Res Año: 2017 Tipo del documento: Article País de afiliación: India Pais de publicación: Reino Unido