Hierarchical mechanism of amino acid sensing by the T-box riboswitch

In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis. Co-transcriptional binding of an uncharged tRNA to the riboswitch stabilizes an antiterminator, allowing transcription read-through, whereas...

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Published inNature communications Vol. 9; no. 1; pp. 1896 - 14
Main Authors Suddala, Krishna C., Cabello-Villegas, Javier, Michnicka, Malgorzata, Marshall, Collin, Nikonowicz, Edward P., Walter, Nils G.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 14.05.2018
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Abstract In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis. Co-transcriptional binding of an uncharged tRNA to the riboswitch stabilizes an antiterminator, allowing transcription read-through, whereas an aminoacylated tRNA does not. Recent structural studies have resolved two contact points between tRNA and Stem-I in the 5′ half of the T-box riboswitch, but little is known about the mechanism empowering transcriptional control by a small, distal aminoacyl modification. Using single-molecule fluorescence microscopy, we have probed the kinetic and structural underpinnings of tRNA binding to a glycyl T-box riboswitch. We observe a two-step mechanism where fast, dynamic recruitment of tRNA by Stem-I is followed by ultra-stable anchoring by the downstream antiterminator, but only without aminoacylation. Our results support a hierarchical sensing mechanism wherein dynamic global binding of the tRNA body is followed by localized readout of its aminoacylation status by snap-lock-based trapping. Riboswitches on 5′ ends of mRNAs are important for bacterial gene regulation. Here the authors probe the mechanism of a tRNA aminoacylation sensing T-box riboswitch using single-molecule fluorescence microscopy to characterize dynamic solution conformations and heterogeneous tRNA binding kinetics.
AbstractList In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis. Co-transcriptional binding of an uncharged tRNA to the riboswitch stabilizes an antiterminator, allowing transcription read-through, whereas an aminoacylated tRNA does not. Recent structural studies have resolved two contact points between tRNA and Stem-I in the 5′ half of the T-box riboswitch, but little is known about the mechanism empowering transcriptional control by a small, distal aminoacyl modification. Using single-molecule fluorescence microscopy, we have probed the kinetic and structural underpinnings of tRNA binding to a glycyl T-box riboswitch. We observe a two-step mechanism where fast, dynamic recruitment of tRNA by Stem-I is followed by ultra-stable anchoring by the downstream antiterminator, but only without aminoacylation. Our results support a hierarchical sensing mechanism wherein dynamic global binding of the tRNA body is followed by localized readout of its aminoacylation status by snap-lock-based trapping. Riboswitches on 5′ ends of mRNAs are important for bacterial gene regulation. Here the authors probe the mechanism of a tRNA aminoacylation sensing T-box riboswitch using single-molecule fluorescence microscopy to characterize dynamic solution conformations and heterogeneous tRNA binding kinetics.
Riboswitches on 5′ ends of mRNAs are important for bacterial gene regulation. Here the authors probe the mechanism of a tRNA aminoacylation sensing T-box riboswitch using single-molecule fluorescence microscopy to characterize dynamic solution conformations and heterogeneous tRNA binding kinetics.
In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis. Co-transcriptional binding of an uncharged tRNA to the riboswitch stabilizes an antiterminator, allowing transcription read-through, whereas an aminoacylated tRNA does not. Recent structural studies have resolved two contact points between tRNA and Stem-I in the 5' half of the T-box riboswitch, but little is known about the mechanism empowering transcriptional control by a small, distal aminoacyl modification. Using single-molecule fluorescence microscopy, we have probed the kinetic and structural underpinnings of tRNA binding to a glycyl T-box riboswitch. We observe a two-step mechanism where fast, dynamic recruitment of tRNA by Stem-I is followed by ultra-stable anchoring by the downstream antiterminator, but only without aminoacylation. Our results support a hierarchical sensing mechanism wherein dynamic global binding of the tRNA body is followed by localized readout of its aminoacylation status by snap-lock-based trapping.
ArticleNumber 1896
Author Suddala, Krishna C.
Nikonowicz, Edward P.
Walter, Nils G.
Michnicka, Malgorzata
Cabello-Villegas, Javier
Marshall, Collin
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  givenname: Javier
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  organization: Single Molecule Analysis Group, Department of Chemistry, University of Michigan
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  surname: Marshall
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  organization: Single Molecule Analysis Group, Department of Chemistry, University of Michigan
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  givenname: Edward P.
  surname: Nikonowicz
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  surname: Walter
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  email: nwalter@umich.edu
  organization: Single Molecule Analysis Group, Department of Chemistry, University of Michigan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29760498$$D View this record in MEDLINE/PubMed
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Snippet In Gram-positive bacteria, T-box riboswitches control gene expression to maintain the cellular pools of aminoacylated tRNAs essential for protein biosynthesis....
Riboswitches on 5′ ends of mRNAs are important for bacterial gene regulation. Here the authors probe the mechanism of a tRNA aminoacylation sensing T-box...
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StartPage 1896
SubjectTerms 631/57/2265
631/92/500
Amino acids
Aminoacylation
Anchoring
Base Pairing
Binding
Biosynthesis
Chemoreception
Downstream effects
Fluorescence
Fluorescence microscopy
Gene expression
Gene Expression Regulation, Bacterial
Gram-positive bacteria
Gram-Positive Bacteria - genetics
Gram-Positive Bacteria - metabolism
Humanities and Social Sciences
Microscopy, Fluorescence
Molecular chains
multidisciplinary
Nucleic Acid Conformation
Protein Biosynthesis
Proteins
Riboswitch
Riboswitches
RNA, Bacterial - chemistry
RNA, Bacterial - genetics
RNA, Bacterial - metabolism
RNA, Transfer - chemistry
RNA, Transfer - genetics
RNA, Transfer - metabolism
Science
Science (multidisciplinary)
Single Molecule Imaging
Transcription
Transfer RNA Aminoacylation
tRNA
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Title Hierarchical mechanism of amino acid sensing by the T-box riboswitch
URI https://link.springer.com/article/10.1038/s41467-018-04305-6
https://www.ncbi.nlm.nih.gov/pubmed/29760498
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https://search.proquest.com/docview/2039296477
https://pubmed.ncbi.nlm.nih.gov/PMC5951919
https://doaj.org/article/311b4e87aa5d46d280d8e1c2f066cf5b
Volume 9
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