Proceedings of the National Academy of Sciences · 1985 · 348 citations · 37 references
Life SciencesBiochemistryMolecular BiologyDna ReplicationNucleic Acid BiochemistryTranscriptionProtein Sequence AnalysisRna Polymerase StructureRna TranscriptionAmino Acid Composition AnalysisC-terminal Domain StructureEukaryotic Rna Polymerase Ii StructurePhosphorylation Of The Rna Polymerase Ii C-terminal DomainPolymerase Subunit OrganizationRna Polymerase Ii FunctionRna Polymerase Subunit Architecture
Purified eukaryotic nuclear RNA polymerase II consists of three subspecies that differ in the apparent molecular masses of their largest subunit, designated IIo, IIa, and IIb for polymerase species IIO, IIA, and IIB, respectively. Subunits IIo, IIa, and IIb are the products of a single gene. We present here the amino acid composition of calf thymus subunits IIa and IIb and the C-terminal amino acid sequence of subunit IIa (IIo) inferred from the nucleotide sequence of part of the mouse gene encoding this RNA polymerase subunit. The calculated amino acid composition of the peptide unique to subunit IIa indicates that subunit IIa contains a domain rich in serine, proline, threonine, and tyrosine. The sequence at the 3' end of the mouse RNA polymerase II largest subunit gene reveals that the C-terminal domain consists of 52 repeats of a seven amino acid block with the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser. This sequence is also unusual in that it contains a high percentage of potential phosphorylation sites.
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Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
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