| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| A conserved motif common to the histone acetyltransferase Esa 1 and the histone deacetylase Rpd 3 . ^^^ A particular pair of HAT ( Esa 1 ) and HDAC ( Rpd 3 ) is proposed to modify the same lysine residue in vitro and in vivo . ^^^ Here we show that HAT ( Esa 1 family ) and HDAC ( Rpd 3 family ) have similar amino acid stretches in the primary structures through evolution . ^^^ In Rpd 3 , for which the tertiary structure remains unclear , we demonstrate that the ER motif contains the same secondary structure as found in Esa 1 by circular dichroism analysis . ^^^ We did alanine scanning mutagenesis and found that the ER motif regions of Esa 1 or Rpd 3 are required for HAT activity of Esa 1 or HDAC activity of Rpd 3 , respectively . ^^^ |
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| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| Furthermore , the histone acetyltransferases Gcn 5 and Esa 1 and the histone deacetylases Rpd 3 , Sir 2 , and Hst 1 are recruited to the HO lesion during homologous recombinational repair . ^^^ |
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| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| Here we show that this region is acetylated extensively by ESA 1 and GCN 5 and deacetylated by HDA 1 and RPD 3 , and that widespread histone modification affects three separate chromosomal regions examined , which total 22kb . ^^^ |
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| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| At the INO 1 promoter , RPD 3 is required for strongly deacetylating all sites except H 4 K16 , ESA 1 for acetylating H2A , H2B , and H 4 sites except H 4 K16 , and GCN 5 for acetylating H2B and H 3 sites except H 3 K14 . ^^^ |
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| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q92769 and Q92993 |
Pubmed |
SVM Score :0.0 |
| NA |
|