Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2000-12-12
pubmed:abstractText
Utilizing a novel and rapid two-column purification procedure, the DNA-dependent RNA polymerase (RNAP) from the thermophile, Thermus thermophilus HB8, was purified to electrophoretic homogeneity with a recovery of 65% (as determined by RNAP activity) in less than 2 days. The purified enzyme was characterized using DNA containing the lambdaP(R) promoter. KMnO(4) footprinting, abortive initiation assays, and the formation of the specific stalled elongation complex provide compelling evidence that T. thermophilus RNA polymerase can bind to DNA containing the lambdaP(R) promoter, form an open complex, and initiate transcription in a temperature-dependent manner. This evidence suggests that T. thermophilus RNAP possesses less intrinsic binding energy than E. coli RNAP. Instead, T. thermophilus relies on the high temperatures of its environment to provide the thermal energy required to stimulate open promoter complex formation, initiate transcription, and facilitate the conformational changes in RNA polymerase that result in nucleotide incorporation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14356-62
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Purification and initial characterization of RNA polymerase from Thermus thermophilus strain HB8.
pubmed:affiliation
Department of Chemistry, Campus Box 3290, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3290, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't