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Processing of A-form ssDNA by cryptic RNase H fold exonuclease PF2046
- Authors
- Kim, Junsoo; Sambalkhundev, Gerelt-Od; Kim, Sulhee; Son, Jonghyeon; Han, Ah-reum; Ko, Sul-Min; Hwang, Kwang Yeon; Lee, Woo Cheol
- Issue Date
- 15-Sep-2016
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Exonuclease; ssDNA; A-form; RNase H
- Citation
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.606, pp.143 - 150
- Indexed
- SCIE
SCOPUS
- Journal Title
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Volume
- 606
- Start Page
- 143
- End Page
- 150
- ISSN
- 0003-9861
- Abstract
- RNase H fold protein PF2046 of Pyrococcus furiosus is a 3'-5' ssDNA exonuclease that cleaves after the second nucleotide from the 3' end of ssDNA and prefers poly-dT over poly-dA as a substrate. In our crystal structure of PF2046 complexed with an oligonucleotide of four thymidine nucleotides (dT(4)), PF2046 accommodates dT(4) tightly in a groove and imposes steric hindrance on dT(4) mainly by Phe220 such that dT(4) assumes the A-form. As poly-dA prefer B-form due to the stereochemical restrictions, the A-form ssDNA binding by PF2046 should disfavor the processing of poly-dA. Phe220 variants display reduced activity toward poly-dA and the A-form appears to be a prerequisite for the processing by PF2046. (C) 2016 Elsevier Inc. All rights reserved.
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Related Researcher
- Hwang, Kwang Yeon
- Department of Biotechnology