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Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
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| Zeitschriftentitel: | Genes & Development |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Genes & Development, 17, 2003, 15, S. 1823-1828 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
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| Schlagwörter: |
| author_facet |
Min, Jinrong Zhang, Yi Xu, Rui-Ming Min, Jinrong Zhang, Yi Xu, Rui-Ming |
|---|---|
| author |
Min, Jinrong Zhang, Yi Xu, Rui-Ming |
| spellingShingle |
Min, Jinrong Zhang, Yi Xu, Rui-Ming Genes & Development Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 Developmental Biology Genetics |
| author_sort |
min, jinrong |
| spelling |
Min, Jinrong Zhang, Yi Xu, Rui-Ming 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.269603 <jats:p>The chromodomain of<jats:italic>Drosophila</jats:italic>Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-Å-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.</jats:p> Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 Genes & Development |
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10.1101/gad.269603 |
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Cold Spring Harbor Laboratory, 2003 |
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| title |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_unstemmed |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_full |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_fullStr |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_full_unstemmed |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_short |
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_sort |
structural basis for specific binding of polycomb chromodomain to histone h3 methylated at lys 27 |
| topic |
Developmental Biology Genetics |
| url |
http://dx.doi.org/10.1101/gad.269603 |
| publishDate |
2003 |
| physical |
1823-1828 |
| description |
<jats:p>The chromodomain of<jats:italic>Drosophila</jats:italic>Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-Å-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.</jats:p> |
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| author | Min, Jinrong, Zhang, Yi, Xu, Rui-Ming |
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| description | <jats:p>The chromodomain of<jats:italic>Drosophila</jats:italic>Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-Å-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.</jats:p> |
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| spelling | Min, Jinrong Zhang, Yi Xu, Rui-Ming 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.269603 <jats:p>The chromodomain of<jats:italic>Drosophila</jats:italic>Polycomb protein is essential for maintaining the silencing state of homeotic genes during development. Recent studies suggest that Polycomb mediates the assembly of repressive higher-order chromatin structures in conjunction with the methylation of Lys 27 of histone H3 by a Polycomb group repressor complex. A similar mechanism in heterochromatin assembly is mediated by HP1, a chromodomain protein that binds to histone H3 methylated at Lys 9. To understand the molecular mechanism of the methyl-Lys 27 histone code recognition, we have determined a 1.4-Å-resolution structure of the chromodomain of Polycomb in complex with a histone H3 peptide trimethylated at Lys 27. The structure reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3. The structure also reveals a dPC dimer in the crystal lattice that is mediated by residues specifically conserved in the Polycomb family of chromodomains. The dimerization of dPC can effectively account for the histone-binding specificity and provides new mechanistic insights into the function of Polycomb. We propose that self-association is functionally important for Polycomb.</jats:p> Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 Genes & Development |
| spellingShingle | Min, Jinrong, Zhang, Yi, Xu, Rui-Ming, Genes & Development, Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27, Developmental Biology, Genetics |
| title | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_full | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_fullStr | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_full_unstemmed | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_short | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| title_sort | structural basis for specific binding of polycomb chromodomain to histone h3 methylated at lys 27 |
| title_unstemmed | Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27 |
| topic | Developmental Biology, Genetics |
| url | http://dx.doi.org/10.1101/gad.269603 |