期刊
NUCLEIC ACIDS RESEARCH
卷 39, 期 2, 页码 536-544出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq791
关键词
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资金
- Cooperative State Research, Education and Extension Service/US Department of Agriculture [SC-1700274, 5767]
- Department of Defense [W911NF-05-1-0335, W911NF-07-1-0141, W81XWH-10-1-0385]
- National Institutes of Health [GM090141]
- Calhoun Honors College of Clemson University
- Howard Hughes Medical Institute
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R15GM090141] Funding Source: NIH RePORTER
Endonuclease V is an enzyme that initiates a conserved DNA repair pathway by making an endonucleolytic incision at the 3'-side 1 nt from a deaminated base lesion. DNA cleavage analysis using mutants defective in DNA binding and Mn2+ as a metal cofactor reveals a novel 3'-exonuclease activity in endonuclease V [Feng,H., Dong,L., Klutz,A.M., Aghaebrahim,N. and Cao,W. (2005) Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V. Biochemistry, 44, 11486-11495.]. This study defines the enzymatic nature of the endonuclease and exonuclease activity in endonuclease V from Thermotoga maritima. In addition to its well-known inosine-dependent endonuclease, Tma endonuclease V also exhibits inosine-dependent 3'-exonuclease activity. The dependence on an inosine site and the exonuclease nature of the 3'-exonuclease activity was demonstrated using 5'-labeled and internally-labeled inosine-containing DNA and a H214D mutant that is defective in non-specific nuclease activity. Detailed kinetic analysis using 3'-labeled DNA indicates that Tma endonuclease V also possesses non-specific 5'-exonuclease activity. The multiplicity of the endonuclease and exonuclease activity is discussed with respect to deaminated base repair.
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