Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome

Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we ide...
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Gespeichert in:

Autor*in:	Ticu, Cristina [verfasserIn] Nechifor, Roxana [verfasserIn] Nguyen, Boray [verfasserIn] Desrosiers, Melanie [verfasserIn] Wilson, Kevin S [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2009

Schlagwörter:	elongation factor GTP hydrolysis ribosome translation

Anmerkung:	© European Molecular Biology Organization 2009

Übergeordnetes Werk:	Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 28(2009), 14 vom: 18. Juni, Seite 2053-2065
Übergeordnetes Werk:	volume:28 ; year:2009 ; number:14 ; day:18 ; month:06 ; pages:2053-2065

Links:	Volltext

DOI / URN:	10.1038/emboj.2009.169

Katalog-ID:	SPR057861366

Internformat


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100	1		\|a Ticu, Cristina \|e verfasserin \|4 aut
245	1	0	\|a Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
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520			\|a Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis.
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700	1		\|a Wilson, Kevin S \|e verfasserin \|4 aut
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912			\|a GBV_ILN_32
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_72
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_168
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_252
912			\|a GBV_ILN_266
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
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_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
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_2018
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_2037
912			\|a GBV_ILN_2038
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_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4029
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4126
912			\|a GBV_ILN_4155
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
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_4328
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4367
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
951			\|a AR
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Indexfelder

author_variant	c t ct r n rn b n bn m d md k s w ks ksw
matchkey_str	article:14602075:2009----::ofrainlhneisiciffdietdrcinlyln
hierarchy_sort_str	2009
publishDate	2009
allfields	10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 28 2009 14 18 06 2053-2065
spelling	10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 28 2009 14 18 06 2053-2065
allfields_unstemmed	10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 28 2009 14 18 06 2053-2065
allfieldsGer	10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 28 2009 14 18 06 2053-2065
allfieldsSound	10.1038/emboj.2009.169 doi (DE-627)SPR057861366 (SPR)emboj.2009.169-e DE-627 ger DE-627 rakwb eng Ticu, Cristina verfasserin aut Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213 Nechifor, Roxana verfasserin aut Nguyen, Boray verfasserin aut Desrosiers, Melanie verfasserin aut Wilson, Kevin S verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 28(2009), 14 vom: 18. Juni, Seite 2053-2065 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065 https://dx.doi.org/10.1038/emboj.2009.169 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 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_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 28 2009 14 18 06 2053-2065
language	English
source	Enthalten in The EMBO Journal 28(2009), 14 vom: 18. Juni, Seite 2053-2065 volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065
sourceStr	Enthalten in The EMBO Journal 28(2009), 14 vom: 18. Juni, Seite 2053-2065 volume:28 year:2009 number:14 day:18 month:06 pages:2053-2065
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	elongation factor GTP hydrolysis ribosome translation
isfreeaccess_bool	false
container_title	The EMBO Journal
authorswithroles_txt_mv	Ticu, Cristina @@aut@@ Nechifor, Roxana @@aut@@ Nguyen, Boray @@aut@@ Desrosiers, Melanie @@aut@@ Wilson, Kevin S @@aut@@
publishDateDaySort_date	2009-06-18T00:00:00Z
hierarchy_top_id	266022529
id	SPR057861366
language_de	englisch
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author	Ticu, Cristina
spellingShingle	Ticu, Cristina misc elongation factor misc GTP hydrolysis misc ribosome misc translation Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
authorStr	Ticu, Cristina
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topic_title	Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome elongation factor (dpeaa)DE-He213 GTP hydrolysis (dpeaa)DE-He213 ribosome (dpeaa)DE-He213 translation (dpeaa)DE-He213
topic	misc elongation factor misc GTP hydrolysis misc ribosome misc translation
topic_unstemmed	misc elongation factor misc GTP hydrolysis misc ribosome misc translation
topic_browse	misc elongation factor misc GTP hydrolysis misc ribosome misc translation
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
ctrlnum	(DE-627)SPR057861366 (SPR)emboj.2009.169-e
title_full	Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
author_sort	Ticu, Cristina
journal	The EMBO Journal
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author_browse	Ticu, Cristina Nechifor, Roxana Nguyen, Boray Desrosiers, Melanie Wilson, Kevin S
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format_se	Elektronische Aufsätze
author-letter	Ticu, Cristina
doi_str_mv	10.1038/emboj.2009.169
author2-role	verfasserin
title_sort	conformational changes in switch i of ef‐g drive its directional cycling on and off the ribosome
title_auth	Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
abstract	Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009
abstractGer	Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009
abstract_unstemmed	Abstract We have trapped elongation factor G (EF‐G) from Escherichia coli in six, functionally defined states, representing intermediates in its unidirectional catalytic cycle, which couples GTP hydrolysis to tRNA–mRNA translocation in the ribosome. By probing EF‐G with trypsin in each state, we identified a substantial conformational change involving its conserved switch I (sw1) element, which contacts the GTP substrate. By attaching FeBABE (a hydroxyl radical generating probe) to sw1, we could monitor sw1 movement (by ∼20 Å), relative to the 70S ribosome, during the EF‐G cycle. In free EF‐G, sw1 is disordered, particularly in GDP‐bound and nucleotide‐free states. On EF‐G•GTP binding to the ribosome, sw1 becomes structured and tucked inside the ribosome, thereby locking GTP onto EF‐G. After hydrolysis and translocation, sw1 flips out from the ribosome, greatly accelerating release of GDP and EF‐G from the ribosome. Collectively, our results support a central role of sw1 in driving the EF‐G cycle during protein synthesis. © European Molecular Biology Organization 2009
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container_issue	14
title_short	Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome
url	https://dx.doi.org/10.1038/emboj.2009.169
remote_bool	true
author2	Nechifor, Roxana Nguyen, Boray Desrosiers, Melanie Wilson, Kevin S
author2Str	Nechifor, Roxana Nguyen, Boray Desrosiers, Melanie Wilson, Kevin S
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doi_str	10.1038/emboj.2009.169
up_date	2024-10-18T04:52:21.841Z
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Conformational changes in switch I of EF‐G drive its directional cycling on and off the ribosome

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