Interaction between MRG15 and Methylated Histone H3K36 Studied by NMR Spectroscopy

Abstract

Abstract:

Human MRG15 is a transcription factor that plays an important role in embryonic development, cell proliferation and senescence. The MRG15 chromo domain can interact with methylated Lys36 of histone H3. In this study, the assignment of amino acids of MRG15 chromo domain was done using solution NMR spectroscopy. The interaction between MRG15 chromo domain and H3K36me3 peptide was studied by the chemical shift perturbation approach. The binding sites (i.e., H21，Y46，W49 and W53) and dissociation constants (~1 mmol/L) were determined. These results provide give insight on the interaction between MRG15 chromo domain and histone H3 at molecular level.

Key words: NMR, protein interaction, HSQC, MRG15, chemical shift perturbation

CLC Number:

Q518.2

HONG Jing, LIU Hua, YU Shi-Hong, CHEN Tao-Tao, LIN Dong-Hai. Interaction between MRG15 and Methylated Histone H3K36 Studied by NMR Spectroscopy[J]. Chinese Journal of Magnetic Resonance, 2012, 29(4): 598-604.

References

[1] Pena A N, Tominaga K and Pereira-Smith O M. MRG15 activates the cdc2 promoter via histone acetylation in human cells[J]. Exp Cell Res, 2011, 317(11): 1 534-1 540.

[2] Leung J K, Berube N, Venable S, et al. MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14[J]. J Biol Chem, 2001, 276(42): 39 171-39 178.

[3] Tominaga K, Kirtane B, Jackson J G, et al. MRG15 regulates embryonic development and cell proliferation[J]. Mol Cell Biol, 2005, 25(8): 2 924-2 937.

[4] Carrozza M J, Li B, Florens L, et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription[J]. Cell, 2005, 123(4): 581-592.

[5] Dombecki C R, Chiang A C, Kang H J, et al. The chromodomain protein MRG-1 facilitates SC-independent homologous pairing during meiosis in Caenorhabditis elegans[J]. Dev Cell, 2011, 21(6): 1 092-1 103.

[6] Xu C, Cui G, Botuyan M V, et al. Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S[J]. Structure, 2008, 16(11): 1 740-1 750.

[7] Zhang Nai-xia(张乃霞), Wu Juan(吴娟), Zhang Hua-qun(张华群), et al. Protein-protein interactions studied by NMR A review using the ubiquitin-proteasome NMR(技术在蛋白质-蛋白质相互作用研究中的应用-泛素-蛋白水解酶体通路研究实例介绍)[J]. Chinese J Magn Reson(波谱学杂志), 2012, 29(29): 182-189.

[8] Zhang P, Du J, Sun B, et al. Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3[J]. Nucleic Acids Res, 2006, 34(22): 6 621-6 628.

[9] Delaglio F, Grzesiek S, Vuister G W, et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes[J]. J Biomol NMR, 1995, 6(3): 277-293.

[10] Nilges M, Macias M J, O'Donoghue S I, et al. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin[J]. J Mol Biol, 1997, 269(3): 408-422.

[11] Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures[J]. J Mol Graph, 1996, 14(1): 51-55, 29-32.

[12] Lin Dong-hai(林东海), Hong Jing(洪晶). Mapping protein-ligand interaction by NMR techniques(用NMR技术研究蛋白质一配体相互作用)[J]. Chinese J Magn Reson(波谱学杂志), 2005, 22(3): 321-341.

[13] Wen Yi(文祎), Lin Dong-hai(林东海). Protein dynamics studied by NMR spin relaxation(基于NMR自旋弛豫技术的蛋白质动力学研究)[J]. Chinese J Magn Reson(波谱学杂志), 2012, 29(2): 288-306.

[1]	LIU Wen-qing, SONG Yan-hong, WANG Xue-lu, YAO Ye-feng. In Operando Nuclear Magnetic Resonance Spectroscopy Study on Photocatalytic Methanol Reforming [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 298-308.
[2]	YIN Tian-peng, WANG Ya-rong, WANG Min, SHI Wen-zhi, ZHANG Zheng-qian, HE Sha-sha. Complete Assignments of NMR Spectral Data of Three C₁₉-Diterpenoid Alkaloids [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 331-340.
[3]	YANG Yun-han, DU Yao, YING Fei-xiang, YANG Jun-li, XIA Da-zhen, XIA Fu-ting, YANG Li-juan. Inclusion Behavior of Naringenin/β-Cyclodextrin Supramolecular Complex [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 319-330.
[4]	HU Kun, SUN Han-dong, PUNO Pema-tenzin. Application of Quantum Chemical Calculation of Nuclear Magnetic Resonance Parameters in the Structure Elucidation of Natural Products [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 359-376.
[5]	WANG Ya-lan, WANG Xiao-jing, WANG Zhi-wei. Spectral Analyses and Structural Elucidation of Azilsartan [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 350-358.
[6]	LIU Ji-hong, JIN Kun, WANG Ping, LUO Gen. An NMR Study on Esculetin and It's Derivatives [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 341-349.
[7]	WAN Zhi-bin, SONG Jian-hui, GUO Ming-ming. The Application of in Operando Liquid State NMR on Macromolecular Material Characterization [J]. Chinese Journal of Magnetic Resonance, 2019, 36(3): 408-424.
[8]	TANG Ming-xue, SCHMIDT Claudia. Estimation of Nematic Order Parameters via Haller Analysis of ¹H NMR Spectra of Liquid Crystals [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 138-147.
[9]	CAO Yuan, WU Yong-ping, CHEN Dong-jun. A Spectroscopic Study on Tautomerism of Selaginellins from Selaginella [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 155-163.
[10]	TANG Heng, Gilbert NSHOGOZA, LIU Ming-qing, LIU Ya-qian, RUAN Ke, MA Rong-sheng, GAO Jia. Identification of Novel Hits of the NSD1 SET Domain by NMR Fragment-Based Screening [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 148-154.
[11]	CHEN Xiao-ying, YU Gang-jin, MAO Shi-zhen, LIU Mai-li, DU You-ru. Mixing-Induced Decreases in Critical Micelle Concentration in Aqueous Solution of Surfactants:Probing into the Mechanisms with ¹H NMR Spectroscopy [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 219-224.
[12]	WANG Shuang-hong, ZENG Pei, PAN Si-na, WANG Jia, WANG Shu-mei, YANG Yong-xia. Effects of Gegen Qinlian Decoction on the Fecal Metabonome of High Fructose-Induced Insulin Resistance Rats Studied by ¹H NMR Spectroscopy [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 182-194.
[13]	XIAO Xiong-jie, HU Mary, ZHANG Xu, HU Jian-zhi. An NMR-Based Metabolomics Study of Kidneys from Mice Exposed to Ionizing Radiation [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 172-181.
[14]	XU Xiao-jun, WANG Shen-lin. Probing Membrane Protein Interactions by ¹⁹F Solid-State NMR [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 238-251.
[15]	KOU Xin-hui, LIU Yi-xiang, LIU Xing-hong, LI Cong-gang, LIU Mai-li, JIANG Ling. Visualizing the Pre-Active Conformation of Response Regulator PhoB_N^F20D in Its apo State [J]. Chinese Journal of Magnetic Resonance, 2019, 36(2): 164-171.