Abstract
The Saccharomyces cerevisiae proteins Spt4p, Spt5p and Spt6p are involved in transcriptional repression by modulating the structure of chromatin. From HeLa cells we have purified a human homologue of Spt5p, Supt5hp, and show here that the protein is reversibly phosphorylated in mitosis. The cloned cDNA predicts a protein of 1087 residues with 31% identity to yeast Spt5p. It includes an acidic N-terminus, a putative nuclear localization signal and a C-terminal region containing two different repeated motifs. One of them, with the consensus sequence P-T/S-P-S-P-Q/A-S/G-Y, is similar to the C-terminal domain in the largest subunit of RNA polymerase II.
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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Base Sequence
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Cell Cycle / physiology
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Chromatin / chemistry*
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Chromatin / drug effects
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Chromatin / metabolism*
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Chromosomal Proteins, Non-Histone / chemistry
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Chromosomal Proteins, Non-Histone / genetics
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Chromosomal Proteins, Non-Histone / metabolism*
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Chromosomal Proteins, Non-Histone / pharmacology*
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Cloning, Molecular
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DNA, Complementary / chemistry
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DNA, Complementary / isolation & purification
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HeLa Cells
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Humans
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Mitosis*
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Molecular Sequence Data
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Phosphorylation
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Sequence Homology, Amino Acid
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription Factors / pharmacology*
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Transcriptional Elongation Factors*
Substances
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Chromatin
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Chromosomal Proteins, Non-Histone
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DNA, Complementary
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Transcription Factors
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Transcriptional Elongation Factors
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SPT5 transcriptional elongation factor