Linked Life Data

3031051

Source:http://linkedlifedata.com/resource/pubmed/id/3031051

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1987-5-15
pubmed:abstractText
We have identified tyrosine 122 of the A subunit of Escherichia coli DNA gyrase as the tyrosine that becomes covalently bound to DNA when the enzyme breaks the phosphodiester bonds of DNA. The covalent gyrase X DNA complex was isolated following cleavage of the DNA by gyrase in the presence of the gyrase inhibitor oxolinic acid. The active site tyrosine was first mapped to two overlapping peptides. Its precise position in the sequence of the A subunit of gyrase was then determined by sequencing of a peptide bound to DNA. We also present a method for mapping sites of DNA attachment in a protein of known amino acid sequence. The covalent complex of DNA and protein is treated with proteases that cut specifically. The electrophoretic mobilities of the resulting peptide-bound DNA molecules are correlated with the sizes of the bound peptides, allowing determination of the site of attachment of the DNA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5339-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Mapping the active site tyrosine of Escherichia coli DNA gyrase.
pubmed:publicationType
Journal Article