Linked Life Data

7306497

Source:http://linkedlifedata.com/resource/pubmed/id/7306497

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1982-2-12
pubmed:abstractText
RNA polymerase (RNA nucleotidyltransferase, EC 2.7.7.6) of Agrobacterium tumefaciens has been purified according to a fast and efficient procedure. The method involves only two chromatographic steps and yields a highly active enzyme. The RNA polymerase was studied with respect to the ability to bind its homologous genome. A. tumefaciens deoxyribonucleic acid (DNA) binds the enzyme even when fragmented at undergenic size (300 base pairs). The general binding is unspecific and very labile at low concentrations of heparin (0.66 micrograms/mL). The number and distribution of the stable binding sites, class A sites [Hinkle, D., & Chamberlin, M. J. (1972) J. Mol. Biol. 70, 157-185], have been calculated from the heparin-induced dissociation kinetics of binary complexes formed between the enzyme and DNA fragments of various sizes. A total of 3.5 x 10(3) class A sites (forming binary complexes with a half-life of 16.6 min) are present on A. tumefaciens genome, a large number of which show a distribution of 800-1000 base pairs. The rest have a more widely spaced distribution. The interactions between Escherichia coli RNA polymerase and the A. tumefaciens template have also been examined, and it has been observed that E. coli holoenzyme forms stable complexes with a shorter half-life and recognizes a lower number of class A sites on A. tumefaciens genome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6097-102
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Agrobacterium tumefaciens RNA polymerase: a new purification procedure and a study of the stable binding sites on homologous deoxyribonucleic acid.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't