The Active Site of RNA Polymerase II Participates in Transcript Cleavage Within Arrested Ternary Complexes

RNA polymerase II may become arrested during transcript elongation, in which case the ternary complex remains intact but further RNA synthesis is blocked. To relieve arrest, the nascent transcript must be cleaved from the 3' end. RNAs of 7-17 nt are liberated and transcription continues from th...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 91; no. 17; pp. 8057 - 8061
Main Authors Rudd, Michael D., Izban, Michael G., Luse, Donal S.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 16.08.1994
National Acad Sciences
National Academy of Sciences
Subjects
Active sites
Base Sequence
Binding Sites
Biochemistry
Diphosphates
Diphosphates - pharmacology
Enzymes
Gels
Humans
Kinetics
Legends
Macromolecular Substances
Molecular Sequence Data
Oligodeoxyribonucleotides
Peptide elongation factors
Plasmids
Product labeling
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Ribonucleic acid
Ribonucleotides - metabolism
RNA
RNA Polymerase II - chemistry
RNA Polymerase II - metabolism
Sequencing
Templates, Genetic
Transcription Factors - isolation & purification
Transcription Factors - metabolism
Transcription Factors, General
Transcription, Genetic
Transcriptional Elongation Factors
Truncation
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Summary:RNA polymerase II may become arrested during transcript elongation, in which case the ternary complex remains intact but further RNA synthesis is blocked. To relieve arrest, the nascent transcript must be cleaved from the 3' end. RNAs of 7-17 nt are liberated and transcription continues from the newly exposed 3' end. Factor SII increases elongation efficiency by strongly stimulating the transcript cleavage reaction. We show here that arrest relief can also occur by the addition of pyrophosphate. This generates the same set of cleavage products as factor SII, but the fragments produced with pyrophosphate have 5'-triphosphate termini. Thus, the active site of RNA polymerase II, in the presence of pyrophosphate, appears to be capable of cleaving phosphodiester linkages as far as 17 nt upstream of the original site of polymerization, leaving the ternary complex intact and transcriptionally active.
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.17.8057