http://www.cnr.it/ontology/cnr/individuo/prodotto/ID169530
Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions (Articolo in rivista)
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- Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1093/nar/gkq691 (literal)
- Alternative label
Fantini D, Vascotto C, Marasco D, D'Ambrosio C, Romanello M, Vitagliano L, Pedone C, Poletto M, Cesaratto L, Quadrifoglio F, Scaloni A, Radicella JP, Tell G. (2010)
Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions
in Nucleic acids research
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Fantini D, Vascotto C, Marasco D, D'Ambrosio C, Romanello M, Vitagliano L, Pedone C, Poletto M, Cesaratto L, Quadrifoglio F, Scaloni A, Radicella JP, Tell G. (literal)
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- Nucleic Acids Res. 2010 Dec 1;38(22):8239-56. Epub 2010 Aug 10. (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Biomedical Sciences and Technologies, University of Udine, 33100 Udine, Department of Biological Sciences, University of Naples 'Federico II', Institute of Biostructures and Bioimaging, National Research Council, 80134 Naples, Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy and CEA, Institut de Radiobiologie Cellulaire et Moléculaire, UMR217 CNRS, F-92265 Fontenay-aux-Roses, France. (literal)
- Titolo
- Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions (literal)
- Abstract
- Apurinic/apyrimidinic endonuclease 1 (APE1), an essential protein in mammals, is involved in base excision DNA repair (BER) and in regulation of gene expression, acting as a redox co-activator of several transcription factors. Recent findings highlight a novel role for APE1 in RNA metabolism, which is modulated by nucleophosmin (NPM1). The results reported in this article show that five lysine residues (K24, K25, K27, K31 and K32), located in the APE1 N-terminal unstructured domain, are involved in the interaction of APE1 with both RNA and NPM1, thus supporting a competitive binding mechanism. Data from kinetic experiments demonstrate that the APE1 N-terminal domain also serves as a device for fine regulation of protein catalytic activity on abasic DNA. Interestingly, some of these critical lysine residues undergo acetylation in vivo. These results suggest that protein-protein interactions and/or post-translational modifications involving APE1 N-terminal domain may play important in vivo roles, in better coordinating and fine-tuning protein BER activity and function on RNA metabolism. (literal)
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