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Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions.

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.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

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

doi

10.1093/nar/gkq691

subject

Has Abstract

pub_date

2010-12-01 00:00:00

pages

8239-56

issue

22

eissn

0305-1048

issn

1362-4962

pii

gkq691

journal_volume

38

pub_type

杂志文章

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