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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
Title | Interaction study on human androgen receptor (AR) DNA-binding domain (DBD) and lysine-specific demethylase 1 (LSD1) SWIRM domain |
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Authors | |
Issue Date | 2010 |
Citation | The 2010 Joint Conference of the EUROMAR and 17th International Society of Magnetic Resonance (ISMAR), Florence, Italy, 4-9 July 2010. In Book of Abstracts, 2010, p. 207, abstract no. P142 How to Cite? |
Abstract | Prokaryotic 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). |
Description | Poster Session 7.1: Biological Systems The Book of Abstract can be viewed at: http://www.cerm.unifi.it/wwmr2010/files/Book.pdf |
Persistent Identifier | http://hdl.handle.net/10722/169357 |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lo, KC | en_US |
dc.contributor.author | Zhu, G | en_US |
dc.contributor.author | Sze, KH | en_US |
dc.date.accessioned | 2012-10-18T08:51:03Z | - |
dc.date.available | 2012-10-18T08:51:03Z | - |
dc.date.issued | 2010 | en_US |
dc.identifier.citation | The 2010 Joint Conference of the EUROMAR and 17th International Society of Magnetic Resonance (ISMAR), Florence, Italy, 4-9 July 2010. In Book of Abstracts, 2010, p. 207, abstract no. P142 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/169357 | - |
dc.description | Poster Session 7.1: Biological Systems | - |
dc.description | The Book of Abstract can be viewed at: http://www.cerm.unifi.it/wwmr2010/files/Book.pdf | - |
dc.description.abstract | Prokaryotic 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.language | eng | en_US |
dc.relation.ispartof | Joint EUROMAR 2010 & 17th ISMAR Conference | en_US |
dc.relation.ispartof | WWMR 2010 | - |
dc.title | Interaction study on human androgen receptor (AR) DNA-binding domain (DBD) and lysine-specific demethylase 1 (LSD1) SWIRM domain | en_US |
dc.type | Conference_Paper | en_US |
dc.identifier.email | Sze, KH: khsze@hku.hk | en_US |
dc.identifier.authority | Sze, KH=rp00785 | en_US |
dc.identifier.hkuros | 211860 | en_US |
dc.identifier.spage | 207, abstract no. P142 | en_US |
dc.identifier.epage | 207, abstract no. P142 | en_US |