Reader domain specificity and lysine demethylase-4 family function
KDM4 histone demethylases target specific chromatin regions by a mechanism that is not fully characterised. Here, the authors identify trimethyl-lysine histone-binding preferences for closely related KDM4 double tudor domains and use structural and biochemical information to examine the molecular de...
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| Format: | Article |
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Nature Publishing Group
2016-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms13387 |
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doaj-502865cd91ae47c58370ec2f6dd3787b2021-05-11T10:44:21ZengNature Publishing GroupNature Communications2041-17232016-11-017111510.1038/ncomms13387Reader domain specificity and lysine demethylase-4 family functionZhangli Su0Fengbin Wang1Jin-Hee Lee2Kimberly E. Stephens3Romeo Papazyan4Ekaterina Voronina5Kimberly A. Krautkramer6Ana Raman7Jeremy J. Thorpe8Melissa D. Boersma9Vyacheslav I. Kuznetsov10Mitchell D. Miller11Sean D. Taverna12George N. Phillips13John M. Denu14Wisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonBiosciences at Rice, Rice UniversityWisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of MedicineDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of MedicineDivision of Biological Sciences, University of MontanaWisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of MedicineDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of MedicineWisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonWisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonBiosciences at Rice, Rice UniversityDepartment of Pharmacology and Molecular Sciences, The Johns Hopkins University School of MedicineBiosciences at Rice, Rice UniversityWisconsin Institute for Discovery, Morgridge Institute for Research, University of Wisconsin–MadisonKDM4 histone demethylases target specific chromatin regions by a mechanism that is not fully characterised. Here, the authors identify trimethyl-lysine histone-binding preferences for closely related KDM4 double tudor domains and use structural and biochemical information to examine the molecular details of this interaction.https://doi.org/10.1038/ncomms13387 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Zhangli Su Fengbin Wang Jin-Hee Lee Kimberly E. Stephens Romeo Papazyan Ekaterina Voronina Kimberly A. Krautkramer Ana Raman Jeremy J. Thorpe Melissa D. Boersma Vyacheslav I. Kuznetsov Mitchell D. Miller Sean D. Taverna George N. Phillips John M. Denu |
| spellingShingle |
Zhangli Su Fengbin Wang Jin-Hee Lee Kimberly E. Stephens Romeo Papazyan Ekaterina Voronina Kimberly A. Krautkramer Ana Raman Jeremy J. Thorpe Melissa D. Boersma Vyacheslav I. Kuznetsov Mitchell D. Miller Sean D. Taverna George N. Phillips John M. Denu Reader domain specificity and lysine demethylase-4 family function Nature Communications |
| author_facet |
Zhangli Su Fengbin Wang Jin-Hee Lee Kimberly E. Stephens Romeo Papazyan Ekaterina Voronina Kimberly A. Krautkramer Ana Raman Jeremy J. Thorpe Melissa D. Boersma Vyacheslav I. Kuznetsov Mitchell D. Miller Sean D. Taverna George N. Phillips John M. Denu |
| author_sort |
Zhangli Su |
| title |
Reader domain specificity and lysine demethylase-4 family function |
| title_short |
Reader domain specificity and lysine demethylase-4 family function |
| title_full |
Reader domain specificity and lysine demethylase-4 family function |
| title_fullStr |
Reader domain specificity and lysine demethylase-4 family function |
| title_full_unstemmed |
Reader domain specificity and lysine demethylase-4 family function |
| title_sort |
reader domain specificity and lysine demethylase-4 family function |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2016-11-01 |
| description |
KDM4 histone demethylases target specific chromatin regions by a mechanism that is not fully characterised. Here, the authors identify trimethyl-lysine histone-binding preferences for closely related KDM4 double tudor domains and use structural and biochemical information to examine the molecular details of this interaction. |
| url |
https://doi.org/10.1038/ncomms13387 |
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