TAILIEUCHUNG - Báo cáo khoa học: Physiological truncation and domain organization of a novel uracil-DNA-degrading factor

Uracil in DNA is usually considered to be an error, but it may be used for signaling in Drosophiladevelopment via recognition by a novel uracil-DNA-degrading factor (UDE) [(Bekesi Aet al. (2007) Biochem Biophys Res Commun355, 643–648]. The UDE protein has no detectable similarity to any other uracil-DNA-binding factors, and has no structurally or func-tionally described homologs. | ỊFEBS Journal Physiological truncation and domain organization of a novel uracil-DNA-degrading factor RH l-VI I 1 A t l l I 1 IS I .2 11 I t 7 l l I I 2 3 Maria Pukancsik Angela Békési Eva Klement Eva Hunyadi-Gulyas2 Katalin F. Medzihradszky Jan Kosinski4 5 Janusz M. Bujnicki4 6 Carlos Alfonso7 German Rivas7 and Beata G. Vertessy1 1 Institute of Enzymology BiologicalResearch Center Hungarian Academy of Sciences Budapest Hungary 2 Proteomics Research Group BiologicalResearch Center Hungarian Academy of Sciences Szeged Hungary 3 Department of PharmaceuticalChemistry University of California San Francisco CA USA 4 Laboratory of Bioinformatics and Protein Engineering InternationalInstitute of Molecular and CellBiology Warsaw Poland 5 PhD School Institute of Biochemistry and Biophysics PAS Warsaw Poland 6 Institute of Molecular Biology and Biotechnology Adam Mickiewicz University Poznan Poland 7 Chemicaland PhysicalBiology Centro de Investigaciones Biologicas Madrid Spain Keywords cell death DNA nuclease protein structural modeling uracil Correspondence B. G. Vertessy Institute of Enzymology BiologicalResearch Center Hungarian Academy of Sciences H-1113 Budapest Karolina ut 29 Hungary Fax 36 1 466 5465 Tel 36 1 279 3116 E-mail vertessy@ Received 2 April2009 revised 16 December 2009 accepted 18 December 2009 doi Uracil in DNA is usually considered to be an error but it may be used for signaling in Drosophila development via recognition by a novel uracil-DNA-degrading factor UDE Bekesi A et al. 2007 Biochem Biophys Res Commun 355 643-648 . The UDE protein has no detectable similarity to any other uracil-DNA-binding factors and has no structurally or functionally described homologs. Here a combination of theoretical and experimental analyses reveals the domain organization and DNA-binding pattern of UDE. Sequence alignments and limited proteolysis with different proteases show extensive protection by DNA at the N-terminal duplicated

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