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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
1997-5-8
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pubmed:databankReference | |
pubmed:abstractText |
Stalled Xenopus RNA polymerase I (pol I) elongation complexes bearing a 52-nucleotide RNA were prepared by promoter-initiated transcription in the absence of UTP. When such complexes were isolated and incubated in the presence of Mg2+, the associated RNA was shortened from the 3'-end, and mono- and dinucleotides were released. Shortened transcripts were still associated with the DNA and were quantitatively reelongated upon addition of NTPs. The cleavage activity could be removed from the pol I-ternary complex with buffers containing 0.25% Sarkosyl. These findings indicate that a factor with characteristics similar to elongation factor TFIIS is associated with the pol I elongation complex. However, addition of recombinant Xenopus TFIIS to Sarkosyl-washed pol I elongation complexes had no effect, whereas it showed the expected effects in control reactions with identically prepared pol II elongation complexes. The results thus suggest the existence of a pol I-specific cleavage/elongation factor. I also report the sequence of a novel type of Xenopus TFIIS. The predicted amino acid sequences of the present and previously identified Xenopus TFIIS are less than 65% conserved. Thus, like mammalian species, Xenopus has at least two highly divergent forms of TFIIS.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcosine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, General,
http://linkedlifedata.com/resource/pubmed/chemical/Transcriptional Elongation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/sarkosyl,
http://linkedlifedata.com/resource/pubmed/chemical/transcription factor S-II
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9055-61
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9083031-Amino Acid Sequence,
pubmed-meshheading:9083031-Animals,
pubmed-meshheading:9083031-DNA Polymerase II,
pubmed-meshheading:9083031-Detergents,
pubmed-meshheading:9083031-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9083031-Molecular Sequence Data,
pubmed-meshheading:9083031-Neoplasm Proteins,
pubmed-meshheading:9083031-Peptide Chain Elongation, Translational,
pubmed-meshheading:9083031-RNA Polymerase I,
pubmed-meshheading:9083031-Sarcosine,
pubmed-meshheading:9083031-Transcription, Genetic,
pubmed-meshheading:9083031-Transcription Factors,
pubmed-meshheading:9083031-Transcription Factors, General,
pubmed-meshheading:9083031-Transcriptional Elongation Factors,
pubmed-meshheading:9083031-Xenopus
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pubmed:year |
1997
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pubmed:articleTitle |
Transcript cleavage in an RNA polymerase I elongation complex. Evidence for a dissociable activity similar to but distinct from TFIIS.
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pubmed:affiliation |
Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037, USA. plabhart@scripps.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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