Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon

Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-messenger RNA (tmRNA) to restart translation and lab...
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Autor*in:	David Teran [verfasserIn] Ying Zhang [verfasserIn] Andrei A. Korostelev [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2024

Schlagwörter:	endogenous tmRNA tmRNA decoding A-minor interactions SmpB cryo-EM alanyl-tRNA

Übergeordnetes Werk:	In: Frontiers in Microbiology - Frontiers Media S.A., 2011, 15(2024)
Übergeordnetes Werk:	volume:15 ; year:2024

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fmicb.2024.1369760

Katalog-ID:	DOAJ097067288

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allfieldsSound	10.3389/fmicb.2024.1369760 doi (DE-627)DOAJ097067288 (DE-599)DOAJ0843585891bd4bfc81d5f89c22600307 DE-627 ger DE-627 rakwb eng QR1-502 David Teran verfasserin aut Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-messenger RNA (tmRNA) to restart translation and label the resulting peptide for degradation. Previous studies have visualized how tmRNA and its helper protein SmpB interact with the stalled ribosome to establish a new open reading frame. As tmRNA presents the first alanine codon via a non-canonical mRNA path in the ribosome, the incoming alanyl-tRNA must rearrange the tmRNA molecule to read the codon. Here, we describe cryo-EM analyses of an endogenous Escherichia coli ribosome-tmRNA complex with tRNAAla accommodated in the A site. The flexible adenosine-rich tmRNA linker, which connects the mRNA-like domain with the codon, is stabilized by the minor groove of the canonically positioned anticodon stem of tRNAAla. This ribosome complex can also accommodate a tRNA near the E (exit) site, bringing insights into the translocation and dissociation of the tRNA that decoded the defective mRNA prior to tmRNA binding. Together, these structures uncover a key step of ribosome rescue, in which the ribosome starts translating the tmRNA reading frame. endogenous tmRNA tmRNA decoding A-minor interactions SmpB cryo-EM alanyl-tRNA Microbiology Ying Zhang verfasserin aut Andrei A. Korostelev verfasserin aut In Frontiers in Microbiology Frontiers Media S.A., 2011 15(2024) (DE-627)642889384 (DE-600)2587354-4 1664302X nnns volume:15 year:2024 https://doi.org/10.3389/fmicb.2024.1369760 kostenfrei https://doaj.org/article/0843585891bd4bfc81d5f89c22600307 kostenfrei https://www.frontiersin.org/articles/10.3389/fmicb.2024.1369760/full kostenfrei https://doaj.org/toc/1664-302X 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_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 15 2024
language	English
source	In Frontiers in Microbiology 15(2024) volume:15 year:2024
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topic_facet	endogenous tmRNA tmRNA decoding A-minor interactions SmpB cryo-EM alanyl-tRNA Microbiology
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container_title	Frontiers in Microbiology
authorswithroles_txt_mv	David Teran @@aut@@ Ying Zhang @@aut@@ Andrei A. Korostelev @@aut@@
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callnumber-first	Q - Science
author	David Teran
spellingShingle	David Teran misc QR1-502 misc endogenous tmRNA misc tmRNA decoding misc A-minor interactions misc SmpB misc cryo-EM misc alanyl-tRNA misc Microbiology Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon
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topic_title	QR1-502 Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon endogenous tmRNA tmRNA decoding A-minor interactions SmpB cryo-EM alanyl-tRNA
topic	misc QR1-502 misc endogenous tmRNA misc tmRNA decoding misc A-minor interactions misc SmpB misc cryo-EM misc alanyl-tRNA misc Microbiology
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title	Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon
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title_full	Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon
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title_sort	endogenous trans-translation structure visualizes the decoding of the first tmrna alanine codon
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title_auth	Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon
abstract	Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-messenger RNA (tmRNA) to restart translation and label the resulting peptide for degradation. Previous studies have visualized how tmRNA and its helper protein SmpB interact with the stalled ribosome to establish a new open reading frame. As tmRNA presents the first alanine codon via a non-canonical mRNA path in the ribosome, the incoming alanyl-tRNA must rearrange the tmRNA molecule to read the codon. Here, we describe cryo-EM analyses of an endogenous Escherichia coli ribosome-tmRNA complex with tRNAAla accommodated in the A site. The flexible adenosine-rich tmRNA linker, which connects the mRNA-like domain with the codon, is stabilized by the minor groove of the canonically positioned anticodon stem of tRNAAla. This ribosome complex can also accommodate a tRNA near the E (exit) site, bringing insights into the translocation and dissociation of the tRNA that decoded the defective mRNA prior to tmRNA binding. Together, these structures uncover a key step of ribosome rescue, in which the ribosome starts translating the tmRNA reading frame.
abstractGer	Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-messenger RNA (tmRNA) to restart translation and label the resulting peptide for degradation. Previous studies have visualized how tmRNA and its helper protein SmpB interact with the stalled ribosome to establish a new open reading frame. As tmRNA presents the first alanine codon via a non-canonical mRNA path in the ribosome, the incoming alanyl-tRNA must rearrange the tmRNA molecule to read the codon. Here, we describe cryo-EM analyses of an endogenous Escherichia coli ribosome-tmRNA complex with tRNAAla accommodated in the A site. The flexible adenosine-rich tmRNA linker, which connects the mRNA-like domain with the codon, is stabilized by the minor groove of the canonically positioned anticodon stem of tRNAAla. This ribosome complex can also accommodate a tRNA near the E (exit) site, bringing insights into the translocation and dissociation of the tRNA that decoded the defective mRNA prior to tmRNA binding. Together, these structures uncover a key step of ribosome rescue, in which the ribosome starts translating the tmRNA reading frame.
abstract_unstemmed	Ribosomes stall on truncated or otherwise damaged mRNAs. Bacteria rely on ribosome rescue mechanisms to replenish the pool of ribosomes available for translation. Trans-translation, the main ribosome-rescue pathway, uses a circular hybrid transfer-messenger RNA (tmRNA) to restart translation and label the resulting peptide for degradation. Previous studies have visualized how tmRNA and its helper protein SmpB interact with the stalled ribosome to establish a new open reading frame. As tmRNA presents the first alanine codon via a non-canonical mRNA path in the ribosome, the incoming alanyl-tRNA must rearrange the tmRNA molecule to read the codon. Here, we describe cryo-EM analyses of an endogenous Escherichia coli ribosome-tmRNA complex with tRNAAla accommodated in the A site. The flexible adenosine-rich tmRNA linker, which connects the mRNA-like domain with the codon, is stabilized by the minor groove of the canonically positioned anticodon stem of tRNAAla. This ribosome complex can also accommodate a tRNA near the E (exit) site, bringing insights into the translocation and dissociation of the tRNA that decoded the defective mRNA prior to tmRNA binding. Together, these structures uncover a key step of ribosome rescue, in which the ribosome starts translating the tmRNA reading frame.
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title_short	Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon
url	https://doi.org/10.3389/fmicb.2024.1369760 https://doaj.org/article/0843585891bd4bfc81d5f89c22600307 https://www.frontiersin.org/articles/10.3389/fmicb.2024.1369760/full https://doaj.org/toc/1664-302X
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up_date	2024-07-03T23:37:09.319Z
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Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon

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