The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity
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SCOPUS
- Title
- The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity
- Authors
- Uyen, NT; Park, SY; Choi, JW; Lee, HJ; Nishi, K; Kim, JS; Park, SY; Lee, HJ; Nishi, K
- Date Issued
- 2009-11
- Publisher
- Oxford University Press
- Abstract
- Among four types of bacterial restriction enzymes that cleave a foreign DNA depending on its methylation status, type I enzymes composed of three subunits are interesting because of their unique DNA cleavage and translocation mechanisms performed by the restriction subunit (HsdR). The elucidated N-terminal fragment structure of a putative HsdR subunit from Vibrio vulnificus YJ016 reveals three globular domains. The nucleolytic core within an N-terminal nuclease domain (NTD) is composed of one basic and three acidic residues, which include a metal-binding site. An ATP hydrolase (ATPase) site at the interface of two RecA-like domains (RDs) is located close to the probable DNA-binding site for translocation, which is far from the NTD nucleolytic core. Comparison of relative domain arrangements with other functionally related ATP and/or DNA complex structures suggests a possible translocation and restriction mechanism of the HsdR subunit. Furthermore, careful analysis of its sequence and structure implies that a linker helix connecting two RDs and an extended region within the nuclease domain may play a central role in switching the DNA translocation into the restriction activity.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/109131
- DOI
- 10.1093/nar/gkp603
- ISSN
- 0305-1048
- Article Type
- Article
- Citation
- Nucleic Acids Research, vol. 37, no. 20, page. 6960 - 6969, 2009-11
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