Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro

Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. Ho...
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Autor*in:	Li, Alice Shi Ming [verfasserIn] Homsi, Charles [verfasserIn] Bonneil, Eric [verfasserIn] Thibault, Pierre [verfasserIn] Verreault, Alain [verfasserIn] Vedadi, Masoud [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation

Übergeordnetes Werk:	Enthalten in: Biochimica et biophysica acta / Gene regulatory mechanisms - Amsterdam [u.a.] : Elsevier, 2008, 1866
Übergeordnetes Werk:	volume:1866

DOI / URN:	10.1016/j.bbagrm.2023.194922

Katalog-ID:	ELV010012753

Internformat


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024	7		\|a 10.1016/j.bbagrm.2023.194922 \|2 doi
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100	1		\|a Li, Alice Shi Ming \|e verfasserin \|4 aut
245	1	0	\|a Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
264		1	\|c 2023
336			\|a nicht spezifiziert \|b zzz \|2 rdacontent
337			\|a Computermedien \|b c \|2 rdamedia
338			\|a Online-Ressource \|b cr \|2 rdacarrier
520			\|a Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity.
650		4	\|a Crosstalk
650		4	\|a PRMT1
650		4	\|a Recombinant nucleosome
650		4	\|a Kinetics
650		4	\|a Mass spectrometry
650		4	\|a Arginine methylation
700	1		\|a Homsi, Charles \|e verfasserin \|4 aut
700	1		\|a Bonneil, Eric \|e verfasserin \|4 aut
700	1		\|a Thibault, Pierre \|e verfasserin \|4 aut
700	1		\|a Verreault, Alain \|e verfasserin \|4 aut
700	1		\|a Vedadi, Masoud \|e verfasserin \|4 aut
773	0	8	\|i Enthalten in \|t Biochimica et biophysica acta / Gene regulatory mechanisms \|d Amsterdam [u.a.] : Elsevier, 2008 \|g 1866 \|w (DE-627)557882168 \|w (DE-600)2406725-8 \|w (DE-576)27798128X \|x 1876-4320 \|7 nnns
773	1	8	\|g volume:1866
912			\|a GBV_USEFLAG_U
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912			\|a GBV_ILN_22
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912			\|a GBV_ILN_24
912			\|a GBV_ILN_31
912			\|a GBV_ILN_32
912			\|a GBV_ILN_40
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_151
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4313
912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
936	b	k	\|a 35.70 \|j Biochemie: Allgemeines \|q VZ
936	b	k	\|a 42.12 \|j Biophysik \|q VZ
936	b	k	\|a 42.13 \|j Molekularbiologie \|q VZ
951			\|a AR
952			\|d 1866

Indexfelder

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matchkey_str	article:18764320:2023----::itnhk0ooehltoealseobnnncesmmty
hierarchy_sort_str	2023
bklnumber	35.70 42.12 42.13
publishDate	2023
allfields	10.1016/j.bbagrm.2023.194922 doi (DE-627)ELV010012753 (ELSEVIER)S1874-9399(23)00017-2 DE-627 ger DE-627 rda eng 570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Li, Alice Shi Ming verfasserin aut Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation Homsi, Charles verfasserin aut Bonneil, Eric verfasserin aut Thibault, Pierre verfasserin aut Verreault, Alain verfasserin aut Vedadi, Masoud verfasserin aut Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms Amsterdam [u.a.] : Elsevier, 2008 1866 (DE-627)557882168 (DE-600)2406725-8 (DE-576)27798128X 1876-4320 nnns volume:1866 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.70 Biochemie: Allgemeines VZ 42.12 Biophysik VZ 42.13 Molekularbiologie VZ AR 1866
spelling	10.1016/j.bbagrm.2023.194922 doi (DE-627)ELV010012753 (ELSEVIER)S1874-9399(23)00017-2 DE-627 ger DE-627 rda eng 570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Li, Alice Shi Ming verfasserin aut Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation Homsi, Charles verfasserin aut Bonneil, Eric verfasserin aut Thibault, Pierre verfasserin aut Verreault, Alain verfasserin aut Vedadi, Masoud verfasserin aut Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms Amsterdam [u.a.] : Elsevier, 2008 1866 (DE-627)557882168 (DE-600)2406725-8 (DE-576)27798128X 1876-4320 nnns volume:1866 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.70 Biochemie: Allgemeines VZ 42.12 Biophysik VZ 42.13 Molekularbiologie VZ AR 1866
allfields_unstemmed	10.1016/j.bbagrm.2023.194922 doi (DE-627)ELV010012753 (ELSEVIER)S1874-9399(23)00017-2 DE-627 ger DE-627 rda eng 570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Li, Alice Shi Ming verfasserin aut Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation Homsi, Charles verfasserin aut Bonneil, Eric verfasserin aut Thibault, Pierre verfasserin aut Verreault, Alain verfasserin aut Vedadi, Masoud verfasserin aut Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms Amsterdam [u.a.] : Elsevier, 2008 1866 (DE-627)557882168 (DE-600)2406725-8 (DE-576)27798128X 1876-4320 nnns volume:1866 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.70 Biochemie: Allgemeines VZ 42.12 Biophysik VZ 42.13 Molekularbiologie VZ AR 1866
allfieldsGer	10.1016/j.bbagrm.2023.194922 doi (DE-627)ELV010012753 (ELSEVIER)S1874-9399(23)00017-2 DE-627 ger DE-627 rda eng 570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Li, Alice Shi Ming verfasserin aut Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation Homsi, Charles verfasserin aut Bonneil, Eric verfasserin aut Thibault, Pierre verfasserin aut Verreault, Alain verfasserin aut Vedadi, Masoud verfasserin aut Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms Amsterdam [u.a.] : Elsevier, 2008 1866 (DE-627)557882168 (DE-600)2406725-8 (DE-576)27798128X 1876-4320 nnns volume:1866 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.70 Biochemie: Allgemeines VZ 42.12 Biophysik VZ 42.13 Molekularbiologie VZ AR 1866
allfieldsSound	10.1016/j.bbagrm.2023.194922 doi (DE-627)ELV010012753 (ELSEVIER)S1874-9399(23)00017-2 DE-627 ger DE-627 rda eng 570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Li, Alice Shi Ming verfasserin aut Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro 2023 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity. Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation Homsi, Charles verfasserin aut Bonneil, Eric verfasserin aut Thibault, Pierre verfasserin aut Verreault, Alain verfasserin aut Vedadi, Masoud verfasserin aut Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms Amsterdam [u.a.] : Elsevier, 2008 1866 (DE-627)557882168 (DE-600)2406725-8 (DE-576)27798128X 1876-4320 nnns volume:1866 GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.70 Biochemie: Allgemeines VZ 42.12 Biophysik VZ 42.13 Molekularbiologie VZ AR 1866
language	English
source	Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms 1866 volume:1866
sourceStr	Enthalten in Biochimica et biophysica acta / Gene regulatory mechanisms 1866 volume:1866
format_phy_str_mv	Article
bklname	Biochemie: Allgemeines Biophysik Molekularbiologie
institution	findex.gbv.de
topic_facet	Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation
dewey-raw	570
isfreeaccess_bool	false
container_title	Biochimica et biophysica acta / Gene regulatory mechanisms
authorswithroles_txt_mv	Li, Alice Shi Ming @@aut@@ Homsi, Charles @@aut@@ Bonneil, Eric @@aut@@ Thibault, Pierre @@aut@@ Verreault, Alain @@aut@@ Vedadi, Masoud @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	557882168
dewey-sort	3570
id	ELV010012753
language_de	englisch
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author	Li, Alice Shi Ming
spellingShingle	Li, Alice Shi Ming ddc 570 bkl 35.70 bkl 42.12 bkl 42.13 misc Crosstalk misc PRMT1 misc Recombinant nucleosome misc Kinetics misc Mass spectrometry misc Arginine methylation Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
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topic_title	570 610 VZ 35.70 bkl 42.12 bkl 42.13 bkl Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro Crosstalk PRMT1 Recombinant nucleosome Kinetics Mass spectrometry Arginine methylation
topic	ddc 570 bkl 35.70 bkl 42.12 bkl 42.13 misc Crosstalk misc PRMT1 misc Recombinant nucleosome misc Kinetics misc Mass spectrometry misc Arginine methylation
topic_unstemmed	ddc 570 bkl 35.70 bkl 42.12 bkl 42.13 misc Crosstalk misc PRMT1 misc Recombinant nucleosome misc Kinetics misc Mass spectrometry misc Arginine methylation
topic_browse	ddc 570 bkl 35.70 bkl 42.12 bkl 42.13 misc Crosstalk misc PRMT1 misc Recombinant nucleosome misc Kinetics misc Mass spectrometry misc Arginine methylation
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hierarchy_parent_title	Biochimica et biophysica acta / Gene regulatory mechanisms
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title	Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
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title_full	Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
author_sort	Li, Alice Shi Ming
journal	Biochimica et biophysica acta / Gene regulatory mechanisms
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author_browse	Li, Alice Shi Ming Homsi, Charles Bonneil, Eric Thibault, Pierre Verreault, Alain Vedadi, Masoud
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author-letter	Li, Alice Shi Ming
doi_str_mv	10.1016/j.bbagrm.2023.194922
dewey-full	570 610
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title_sort	histone h4k20 monomethylation enables recombinant nucleosome methylation by prmt1 in vitro
title_auth	Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
abstract	Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity.
abstractGer	Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity.
abstract_unstemmed	Protein arginine methyltransferases (PRMTs) catalyze the transfer of methyl groups to specific arginine residues of histones and nonhistone proteins. There are nine members in the PRMT family (PRMT1 to PRMT9), and PRMT1 is a dominant member catalyzing majority of arginine methylation in the cell. However, none of the PRMTs is active with recombinant nucleosome as substrate in vitro. Here, we report the discovery of the first in class novel crosstalk between histone H4 lysine 20 (H4K20) monomethylation on nucleosome by SETD8 and histone H4 arginine 3 (H4R3) methylation by PRMT1 in vitro. Full kinetic characterization and mass spectrometry analysis indicated that PRMT1 is only active with recombinant nucleosomes monomethylated at H4K20 by SETD8. These data suggests that the level of activity of PRMT1 could potentially be regulated selectively by SETD8 in various pathways, providing a new approach for discovery of selective regulators of PRMT1 activity.
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title_short	Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro
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author2	Homsi, Charles Bonneil, Eric Thibault, Pierre Verreault, Alain Vedadi, Masoud
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doi_str	10.1016/j.bbagrm.2023.194922
up_date	2024-07-07T01:07:19.231Z
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Histone H4K20 monomethylation enables recombinant nucleosome methylation by PRMT1 in vitro

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