Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5205
pubmed:dateCreated
1995-4-14
pubmed:abstractText
Nae I endonuclease must bind to two DNA sequences for cleavage. Examination of the amino acid sequence of Nae I uncovered similarity to the active site of human DNA ligase I, except for leucine 43 in Nae I instead of the lysine essential for ligase activity. Changing leucine 43 to lysine 43 (L43K) changed Nae I activity: Nae I-L43K relaxed supercoiled DNA to yield DNA topoisomers and recombined DNA to give dimeric molecules. Interruption of the reactions of Nae I and Nae I-L43K with DNA demonstrated transient protein-DNA covalent complexes. These findings imply coupled endonuclease and ligase domains and link Nae I endonuclease to the topoisomerase and recombinase protein families.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1817-20
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
DNA topoisomerase and recombinase activities in Nae I restriction endonuclease.
pubmed:affiliation
Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, University of North Carolina Medical School, Chapel Hill 27599.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't