APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process.

ABSTRACT: APE1/Ref-1 (hereafter, APE1), a DNA repair enzyme and a transcriptional coactivator, is a vital protein in mammals. Its role in controlling cell growth and the molecular mechanisms that fine-tune its different cellular functions are still not known. By an unbiased proteomic approach, we have identified and characterized several novel APE1 partners which, unexpectedly, include a number of proteins involved in ribosome biogenesis and RNA processing. In particular, a novel interaction between nucleophosmin (NPM1) and APE1 was characterized. We observed that the 33 N-terminal residues of APE1 are required for stable interaction with the NPM1 oligomerization domain. As a consequence of the interaction with NPM1 and RNA, APE1 is localized within the nucleolus and this localization depends on cel

SUBMITTER: Vascotto C 

PROVIDER: S-EPMC2655621 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature