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Human Supt5h protein, a putative modulator of chromatin structure, is reversibly phosphorylated in mitosis
Author(s) -
Stachora Axel A,
Enrı́quez Schäfer Ramón,
Pohlmeier Matthias,
Maier Gernot,
Ponstingl Herwig
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00486-9
Subject(s) - chromatin , rna polymerase ii , microbiology and biotechnology , biology , mitosis , protein subunit , complementary dna , saccharomyces cerevisiae , c terminus , biochemistry , yeast , dna , gene expression , gene , promoter , amino acid
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.