Abstract
We have investigated the role of the RNA Polymerase II (Pol II) carboxy-terminal domain (CTD) in mRNA 5' capping. Transcripts made in vivo by Pol II with a truncated CTD had a lower proportion of capped 5' ends than those made by Pol II with a full-length CTD. In addition, the enzymes responsible for cap synthesis, RNA guanylyltransferase, and RNA (guanine-7)-methyltransferase bound directly to the phosphorylated, but not to the nonphosphorylated, form of the CTD in vitro. These results suggest that: (1) Pol II-specific capping of nascent transcripts in vivo is enhanced by recruitment of the capping enzymes to the CTD and (2) capping is co-ordinated with CTD phosphorylation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Chloramphenicol O-Acetyltransferase / genetics
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Chloramphenicol O-Acetyltransferase / metabolism
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DNA-Directed RNA Polymerases / metabolism*
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Eukaryotic Initiation Factor-4E
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Globins / genetics
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Globins / metabolism
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Glutathione Transferase / metabolism
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HIV-2 / genetics
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HIV-2 / metabolism
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Humans
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Mammals / genetics
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Methyltransferases / metabolism*
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Mice
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Molecular Sequence Data
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Nucleotidyltransferases / metabolism*
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Peptide Initiation Factors / metabolism
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Phosphorylation
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RNA Caps / metabolism*
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RNA Precursors / metabolism
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RNA Splicing
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RNA, Messenger / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Transcription, Genetic
Substances
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Eukaryotic Initiation Factor-4E
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Peptide Initiation Factors
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RNA Caps
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RNA Precursors
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RNA, Messenger
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Recombinant Proteins
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Globins
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Methyltransferases
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mRNA (guanine(N7))-methyltransferase
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Chloramphenicol O-Acetyltransferase
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Glutathione Transferase
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Nucleotidyltransferases
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mRNA guanylyltransferase
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DNA-Directed RNA Polymerases