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Conference Paper: Interaction study on human androgen receptor (AR) DNA-binding domain (DBD) and lysine-specific demethylase 1 (LSD1) SWIRM domain

TitleInteraction study on human androgen receptor (AR) DNA-binding domain (DBD) and lysine-specific demethylase 1 (LSD1) SWIRM domain
Authors
Issue Date2010
Citation
Joint EUROMAR 2010 and 17th International Society of Magnetic Resonance (ISMAR) Conference, Florence, Italy, 4-9 July 2010. In the Book of Abstract of the Joint EUROMAR 2010 and 17th ISMAR Conference, 2010, p. 207, abstract no, P142 How to Cite?
AbstractProkaryotic and eukaryotic gene regulations are different. Prokaryotic gene regulation requires simply binding of regulatory proteins to help with or avoid forming transcription complex. For eukaryotes like humans, however, their regulation needs “chromatin remodeling” besides association of regulatory proteins, due to the need of opening up DNAhistone protein complex chromatin and unwinding DNA. Without remodeling, RNA polymerases responsible of transcription cannot get access and perform transcription. Lysine-specific demethylase 1 is one of the chromatin remodeling enzymes. It can demethylate specifically the N-tail mono- or di-methylated K4 residue on histone H3 by oxidation.1 LSD1 has three known domains: FAD-binding domain, demethylase domain and SWIRM domain. Till now, the exact function of SWIRM domain of LSD1 is still unclear, although its solution structure is solved and analyzed. In 2005, Metzger’s group found that the LSD1 SWIRM domain could bind the N-terminus, the DNA-binding domain (DBD) and the ligand-binding domain (LBD) of androgen receptor (AR) by GST-pull down assay,2 and showed that SWIRM domain has the strongest interaction among the domains of AR. This study is to investigate the interaction between ARDBD and LSD1 SWIRM domain by NMR techniques. We have carried out chemical shift perturbation titration of N-labeled ARDBD protein with unlabeled SW domain protein. This interaction shows a slow exchange of NMR titration profile. Interacting residues have been mapped onto the structure of ARDBD after backbone resonance assignments on a doubly labeled ARDBD protein sample. References: 1. Shi Y., Lan F., et al., Cell, 119, 941 – 53 (2004) 2. Metzger E., Wissmann M., et al., Nature, 437, 436 – 9 (2005) Acknowledgments: This work was supported by grants from the Hong Kong University Research Grant and the Research Grants Council of Hong Kong for KH Sze (HKU 7533/06M).
DescriptionPoster Session 7.1:Biological Systems
The Book of Abstract can be viewed at: http://www.cerm.unifi.it/wwmr2010/files/Book.pdf
Persistent Identifierhttp://hdl.handle.net/10722/169357

 

DC FieldValueLanguage
dc.contributor.authorLo, KCen_US
dc.contributor.authorZhu, Gen_US
dc.contributor.authorSze, KHen_US
dc.date.accessioned2012-10-18T08:51:03Z-
dc.date.available2012-10-18T08:51:03Z-
dc.date.issued2010en_US
dc.identifier.citationJoint EUROMAR 2010 and 17th International Society of Magnetic Resonance (ISMAR) Conference, Florence, Italy, 4-9 July 2010. In the Book of Abstract of the Joint EUROMAR 2010 and 17th ISMAR Conference, 2010, p. 207, abstract no, P142en_US
dc.identifier.urihttp://hdl.handle.net/10722/169357-
dc.descriptionPoster Session 7.1:Biological Systems-
dc.descriptionThe Book of Abstract can be viewed at: http://www.cerm.unifi.it/wwmr2010/files/Book.pdf-
dc.description.abstractProkaryotic and eukaryotic gene regulations are different. Prokaryotic gene regulation requires simply binding of regulatory proteins to help with or avoid forming transcription complex. For eukaryotes like humans, however, their regulation needs “chromatin remodeling” besides association of regulatory proteins, due to the need of opening up DNAhistone protein complex chromatin and unwinding DNA. Without remodeling, RNA polymerases responsible of transcription cannot get access and perform transcription. Lysine-specific demethylase 1 is one of the chromatin remodeling enzymes. It can demethylate specifically the N-tail mono- or di-methylated K4 residue on histone H3 by oxidation.1 LSD1 has three known domains: FAD-binding domain, demethylase domain and SWIRM domain. Till now, the exact function of SWIRM domain of LSD1 is still unclear, although its solution structure is solved and analyzed. In 2005, Metzger’s group found that the LSD1 SWIRM domain could bind the N-terminus, the DNA-binding domain (DBD) and the ligand-binding domain (LBD) of androgen receptor (AR) by GST-pull down assay,2 and showed that SWIRM domain has the strongest interaction among the domains of AR. This study is to investigate the interaction between ARDBD and LSD1 SWIRM domain by NMR techniques. We have carried out chemical shift perturbation titration of N-labeled ARDBD protein with unlabeled SW domain protein. This interaction shows a slow exchange of NMR titration profile. Interacting residues have been mapped onto the structure of ARDBD after backbone resonance assignments on a doubly labeled ARDBD protein sample. References: 1. Shi Y., Lan F., et al., Cell, 119, 941 – 53 (2004) 2. Metzger E., Wissmann M., et al., Nature, 437, 436 – 9 (2005) Acknowledgments: This work was supported by grants from the Hong Kong University Research Grant and the Research Grants Council of Hong Kong for KH Sze (HKU 7533/06M).-
dc.languageengen_US
dc.relation.ispartofJoint EUROMAR and International Society of Magnetic Resonance (ISMAR) Conferenceen_US
dc.titleInteraction study on human androgen receptor (AR) DNA-binding domain (DBD) and lysine-specific demethylase 1 (LSD1) SWIRM domainen_US
dc.typeConference_Paperen_US
dc.identifier.emailSze, KH: khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.identifier.hkuros211860en_US
dc.identifier.spage207, abstract no, P142en_US
dc.identifier.epage207, abstract no, P142en_US

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