Linked Life Data

6262303

Source:http://linkedlifedata.com/resource/pubmed/id/6262303

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-7-20
pubmed:abstractText
Conditions which result in DNA strand breakage by the rat liver DNA nicking-closing enzyme lead to the covalent attachment of the 3'-end of the broken strand to the enzyme. Treatment of this complex with pancreatic DNase leaves a residue of 17 +/- 8 nucleotide phosphates still attached to the enzyme. Subsequent nuclease P1 treatment removes all but 2 +/- 1 phosphate residues. Using nuclease P1-treated complexes which had been labeled in the DNA with 32P, the stability of the protein-DNA linkage was studied. The linkage is stable to acid, base, neutral and acidic hydroxylamine, and neutral I2. This pattern of stability rules out essentially all of the possible DNA-protein linkages except for a linkage involving a phosphodiester bond to the amino acid tyrosine. After acid hydrolysis of the 32P-labeled complexes, label was found to be associated with O4-phosphotyrosine, providing a direct demonstration that tyrosine is the amino acid to which the end of the DNA chain is attached.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4805-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
DNA is linked to the rat liver DNA nicking-closing enzyme by a phosphodiester bond to tyrosine.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't