Structure of RNA polymerase bound to ribosomal 30S subunit

In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound...
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Autor*in:	Gabriel Demo [verfasserIn] Aviram Rasouly [verfasserIn] Nikita Vasilyev [verfasserIn] Vladimir Svetlov [verfasserIn] Anna B Loveland [verfasserIn] Ruben Diaz-Avalos [verfasserIn] Nikolaus Grigorieff [verfasserIn] Evgeny Nudler [verfasserIn] Andrei A Korostelev [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	RNA polymerase 30S subunit cryo-EM transcription translation coupling

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 6(2017)
Übergeordnetes Werk:	volume:6 ; year:2017

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.28560

Katalog-ID:	DOAJ003330931

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520			\|a In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.
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spelling	10.7554/eLife.28560 doi (DE-627)DOAJ003330931 (DE-599)DOAJf6133fee95ef45eba7820b5d222d7c09 DE-627 ger DE-627 rakwb eng QH301-705.5 Gabriel Demo verfasserin aut Structure of RNA polymerase bound to ribosomal 30S subunit 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation. RNA polymerase 30S subunit cryo-EM transcription translation coupling Medicine R Science Q Biology (General) Aviram Rasouly verfasserin aut Nikita Vasilyev verfasserin aut Vladimir Svetlov verfasserin aut Anna B Loveland verfasserin aut Ruben Diaz-Avalos verfasserin aut Nikolaus Grigorieff verfasserin aut Evgeny Nudler verfasserin aut Andrei A Korostelev verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.28560 kostenfrei https://doaj.org/article/f6133fee95ef45eba7820b5d222d7c09 kostenfrei https://elifesciences.org/articles/28560 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
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allfieldsGer	10.7554/eLife.28560 doi (DE-627)DOAJ003330931 (DE-599)DOAJf6133fee95ef45eba7820b5d222d7c09 DE-627 ger DE-627 rakwb eng QH301-705.5 Gabriel Demo verfasserin aut Structure of RNA polymerase bound to ribosomal 30S subunit 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation. RNA polymerase 30S subunit cryo-EM transcription translation coupling Medicine R Science Q Biology (General) Aviram Rasouly verfasserin aut Nikita Vasilyev verfasserin aut Vladimir Svetlov verfasserin aut Anna B Loveland verfasserin aut Ruben Diaz-Avalos verfasserin aut Nikolaus Grigorieff verfasserin aut Evgeny Nudler verfasserin aut Andrei A Korostelev verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.28560 kostenfrei https://doaj.org/article/f6133fee95ef45eba7820b5d222d7c09 kostenfrei https://elifesciences.org/articles/28560 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
allfieldsSound	10.7554/eLife.28560 doi (DE-627)DOAJ003330931 (DE-599)DOAJf6133fee95ef45eba7820b5d222d7c09 DE-627 ger DE-627 rakwb eng QH301-705.5 Gabriel Demo verfasserin aut Structure of RNA polymerase bound to ribosomal 30S subunit 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation. RNA polymerase 30S subunit cryo-EM transcription translation coupling Medicine R Science Q Biology (General) Aviram Rasouly verfasserin aut Nikita Vasilyev verfasserin aut Vladimir Svetlov verfasserin aut Anna B Loveland verfasserin aut Ruben Diaz-Avalos verfasserin aut Nikolaus Grigorieff verfasserin aut Evgeny Nudler verfasserin aut Andrei A Korostelev verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.28560 kostenfrei https://doaj.org/article/f6133fee95ef45eba7820b5d222d7c09 kostenfrei https://elifesciences.org/articles/28560 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
language	English
source	In eLife 6(2017) volume:6 year:2017
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topic_facet	RNA polymerase 30S subunit cryo-EM transcription translation coupling Medicine R Science Q Biology (General)
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container_title	eLife
authorswithroles_txt_mv	Gabriel Demo @@aut@@ Aviram Rasouly @@aut@@ Nikita Vasilyev @@aut@@ Vladimir Svetlov @@aut@@ Anna B Loveland @@aut@@ Ruben Diaz-Avalos @@aut@@ Nikolaus Grigorieff @@aut@@ Evgeny Nudler @@aut@@ Andrei A Korostelev @@aut@@
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author	Gabriel Demo
spellingShingle	Gabriel Demo misc QH301-705.5 misc RNA polymerase misc 30S subunit misc cryo-EM misc transcription misc translation misc coupling misc Medicine misc R misc Science misc Q misc Biology (General) Structure of RNA polymerase bound to ribosomal 30S subunit
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title	Structure of RNA polymerase bound to ribosomal 30S subunit
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title_full	Structure of RNA polymerase bound to ribosomal 30S subunit
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title_sort	structure of rna polymerase bound to ribosomal 30s subunit
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title_auth	Structure of RNA polymerase bound to ribosomal 30S subunit
abstract	In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.
abstractGer	In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.
abstract_unstemmed	In bacteria, mRNA transcription and translation are coupled to coordinate optimal gene expression and maintain genome stability. Coupling is thought to involve direct interactions between RNA polymerase (RNAP) and the translational machinery. We present cryo-EM structures of E. coli RNAP core bound to the small ribosomal 30S subunit. The complex is stable under cell-like ionic conditions, consistent with functional interaction between RNAP and the 30S subunit. The RNA exit tunnel of RNAP aligns with the Shine-Dalgarno-binding site of the 30S subunit. Ribosomal protein S1 forms a wall of the tunnel between RNAP and the 30S subunit, consistent with its role in directing mRNAs onto the ribosome. The nucleic-acid-binding cleft of RNAP samples distinct conformations, suggesting different functional states during transcription-translation coupling. The architecture of the 30S•RNAP complex provides a structural basis for co-localization of the transcriptional and translational machineries, and inform future mechanistic studies of coupled transcription and translation.
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title_short	Structure of RNA polymerase bound to ribosomal 30S subunit
url	https://doi.org/10.7554/eLife.28560 https://doaj.org/article/f6133fee95ef45eba7820b5d222d7c09 https://elifesciences.org/articles/28560 https://doaj.org/toc/2050-084X
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Structure of RNA polymerase bound to ribosomal 30S subunit

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