DC Field | Value | Language |
---|---|---|
dc.contributor.author | Uyen, NT | - |
dc.contributor.author | Park, SY | - |
dc.contributor.author | Choi, JW | - |
dc.contributor.author | Lee, HJ | - |
dc.contributor.author | Nishi, K | - |
dc.contributor.author | Kim, JS | - |
dc.contributor.author | Park, SY | - |
dc.contributor.author | Lee, HJ | - |
dc.contributor.author | Nishi, K | - |
dc.date.accessioned | 2022-01-10T06:40:13Z | - |
dc.date.available | 2022-01-10T06:40:13Z | - |
dc.date.created | 2021-07-05 | - |
dc.date.issued | 2009-11 | - |
dc.identifier.issn | 0305-1048 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/109131 | - |
dc.description.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. | - |
dc.language | English | - |
dc.publisher | Oxford University Press | - |
dc.relation.isPartOf | Nucleic Acids Research | - |
dc.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 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1093/nar/gkp603 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Nucleic Acids Research, v.37, no.20, pp.6960 - 6969 | - |
dc.identifier.wosid | 000271819900028 | - |
dc.citation.endPage | 6969 | - |
dc.citation.number | 20 | - |
dc.citation.startPage | 6960 | - |
dc.citation.title | Nucleic Acids Research | - |
dc.citation.volume | 37 | - |
dc.contributor.affiliatedAuthor | Park, SY | - |
dc.identifier.scopusid | 2-s2.0-73349100057 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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