Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.

Cell | Aug 18, 2000

http://www.ncbi.nlm.nih.gov/pubmed/10966108

It is well known that histone acetylases are important chromatin modifiers and that they play a central role in chromatin transcription. Here, we present evidence for novel roles of histone acetylases. The TIP60 histone acetylase purifies as a multimeric protein complex. Besides histone acetylase activity on chromatin, the TIP60 complex possesses ATPase, DNA helicase, and structural DNA binding activities. Ectopic expression of mutated TIP60 lacking histone acetylase activity results in cells with defective double-strand DNA break repair. Importantly, the resulting cells lose their apoptotic competence, suggesting a defect in the cells' ability to signal the existence of DNA damage to the apoptotic machinery. These results indicate that the histone acetylase TIP60-containing complex plays a role in DNA repair and apoptosis.

Pubmed ID: 10966108 RIS Download

Mesh terms: Acetyltransferases | Actins | Adenosine Triphosphatases | Apoptosis | Bacterial Proteins | DNA | DNA Helicases | DNA Repair | Electrophoresis, Polyacrylamide Gel | HeLa Cells | Histone Acetyltransferases | Humans | Macromolecular Substances | Molecular Weight | Proteins | Saccharomyces cerevisiae Proteins

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NCI NIH HHS, Id: K01 CA079576

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.