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Friedrich-Heineken, E; Henneke, G; Ferrari, E; Hübscher, U (2003). The acetylatable lysines of human Fen1 are important for endo- and exonuclease activities. Journal of Molecular Biology, 328(1):73-84.

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Abstract

Human Fen1 can be acetylated in vivo and in vitro resulting in reduced endonuclease and exonuclease activities in vitro. Acetylation occurs at four lysines located at the C terminus of Fen1, which is important for DNA binding. In this paper we show that Fen1 mutant proteins lacking the lysines at the C terminus have both reduced PCNA independent exonucleolytic and endonucleolytic activities. However, lysines at the C terminus are not required for PCNA stimulation of human Fen1. A double flap substrate was optimal for human Fen1 endonuclease and did not require the C-terminal lysines. Similarly, a one nucleotide 3'-overhang nick substrate was optimal for human Fen1 exonuclease and also did not require the C-terminal lysines. Finally, we found by an electromobility shift assay that human Fen1 had a different mode of binding with a double flap substrate containing a one nucleotide 3'-tail when compared to various other flap substrates. Taken together, our results confirm the double flap substrate as the likely in vivo intermediate for human Fen1 and that the C-terminal lysines are important for the endonuclease and exonuclease activities likely through DNA binding.

Item Type:Journal Article, refereed
Communities & Collections:05 Vetsuisse Faculty > Institute of Veterinary Biochemistry and Molecular Biology
DDC:570 Life sciences; biology
Language:English
Date:18 April 2003
Deposited On:11 Feb 2008 13:18
Last Modified:28 Nov 2013 02:16
Publisher:Elsevier
ISSN:0022-2836
Publisher DOI:10.1016/S0022-2836(03)00270-5
PubMed ID:12683998
Citations:Web of Science®. Times Cited: 29
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