A UNIQUE STRUCTURE AT THE CARBOXYL TERMINUS OF THE LARGEST SUBUNIT OF EUKARYOTIC RNA POLYMERASE-II

A UNIQUE STRUCTURE AT THE CARBOXYL TERMINUS OF THE LARGEST SUBUNIT OF EUKARYOTIC RNA POLYMERASE-II
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DOI:
10.1073/pnas.82.23.7934
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发表时间:
1985-01-01
影响因子:
11.1
通讯作者:
DAHMUS, ME
DAHMUS, ME
中科院分区:
综合性期刊1区
文献类型:
--
作者:
CORDEN, JL;CADENA, DL;DAHMUS, ME

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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 subnits 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.