T box riboswitches in Actinobacteria: Translational regulation via novel tRNA interactions

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Standard

T box riboswitches in Actinobacteria : Translational regulation via novel tRNA interactions. / Belyaevskaya, Anna; Henkin, Tina; Grundy, Frank.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 112, Nr. 4, 2015, s. 1113-1118.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Belyaevskaya, A, Henkin, T & Grundy, F 2015, 'T box riboswitches in Actinobacteria: Translational regulation via novel tRNA interactions', Proceedings of the National Academy of Sciences of the United States of America, bind 112, nr. 4, s. 1113-1118. https://doi.org/10.1073/pnas.1424175112

APA

Belyaevskaya, A., Henkin, T., & Grundy, F. (2015). T box riboswitches in Actinobacteria: Translational regulation via novel tRNA interactions. Proceedings of the National Academy of Sciences of the United States of America, 112(4), 1113-1118. https://doi.org/10.1073/pnas.1424175112

Vancouver

Belyaevskaya A, Henkin T, Grundy F. T box riboswitches in Actinobacteria: Translational regulation via novel tRNA interactions. Proceedings of the National Academy of Sciences of the United States of America. 2015;112(4):1113-1118. https://doi.org/10.1073/pnas.1424175112

Author

Belyaevskaya, Anna ; Henkin, Tina ; Grundy, Frank. / T box riboswitches in Actinobacteria : Translational regulation via novel tRNA interactions. I: Proceedings of the National Academy of Sciences of the United States of America. 2015 ; Bind 112, Nr. 4. s. 1113-1118.

Bibtex

@article{11871e4847aa4df188d418302f494fa4,
title = "T box riboswitches in Actinobacteria: Translational regulation via novel tRNA interactions",
abstract = "The T box riboswitch regulates many amino acid-related genes in Gram-positive bacteria. T box riboswitch-mediated gene regulation was shown previously to occur at the level of transcription attenuation via structural rearrangements in the 5′ untranslated (leader) region of the mRNA in response to binding of a specific uncharged tRNA. In this study, a novel group of isoleucyl-tRNA synthetase gene (ileS) T box leader sequences found in organisms of the phylum Actinobacteria was investigated. The Stem I domains of these RNAs lack several highly conserved elements that are essential for interaction with the tRNA ligand in other T box RNAs. Many of these RNAs were predicted to regulate gene expression at the level of translation initiation through tRNA-dependent stabilization of a helix that sequesters a sequence complementary to the Shine–Dalgarno (SD) sequence, thus freeing the SD sequence for ribosome binding and translation initiation. We demonstrated specific binding to the cognate tRNAIle and tRNAIle-dependent structural rearrangements consistent with regulation at the level of translation initiation, providing the first biochemical demonstration, to our knowledge, of translational regulation in a T box riboswitch.",
author = "Anna Belyaevskaya and Tina Henkin and Frank Grundy",
year = "2015",
doi = "10.1073/pnas.1424175112",
language = "English",
volume = "112",
pages = "1113--1118",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "4",

}

RIS

TY - JOUR

T1 - T box riboswitches in Actinobacteria

T2 - Translational regulation via novel tRNA interactions

AU - Belyaevskaya, Anna

AU - Henkin, Tina

AU - Grundy, Frank

PY - 2015

Y1 - 2015

N2 - The T box riboswitch regulates many amino acid-related genes in Gram-positive bacteria. T box riboswitch-mediated gene regulation was shown previously to occur at the level of transcription attenuation via structural rearrangements in the 5′ untranslated (leader) region of the mRNA in response to binding of a specific uncharged tRNA. In this study, a novel group of isoleucyl-tRNA synthetase gene (ileS) T box leader sequences found in organisms of the phylum Actinobacteria was investigated. The Stem I domains of these RNAs lack several highly conserved elements that are essential for interaction with the tRNA ligand in other T box RNAs. Many of these RNAs were predicted to regulate gene expression at the level of translation initiation through tRNA-dependent stabilization of a helix that sequesters a sequence complementary to the Shine–Dalgarno (SD) sequence, thus freeing the SD sequence for ribosome binding and translation initiation. We demonstrated specific binding to the cognate tRNAIle and tRNAIle-dependent structural rearrangements consistent with regulation at the level of translation initiation, providing the first biochemical demonstration, to our knowledge, of translational regulation in a T box riboswitch.

AB - The T box riboswitch regulates many amino acid-related genes in Gram-positive bacteria. T box riboswitch-mediated gene regulation was shown previously to occur at the level of transcription attenuation via structural rearrangements in the 5′ untranslated (leader) region of the mRNA in response to binding of a specific uncharged tRNA. In this study, a novel group of isoleucyl-tRNA synthetase gene (ileS) T box leader sequences found in organisms of the phylum Actinobacteria was investigated. The Stem I domains of these RNAs lack several highly conserved elements that are essential for interaction with the tRNA ligand in other T box RNAs. Many of these RNAs were predicted to regulate gene expression at the level of translation initiation through tRNA-dependent stabilization of a helix that sequesters a sequence complementary to the Shine–Dalgarno (SD) sequence, thus freeing the SD sequence for ribosome binding and translation initiation. We demonstrated specific binding to the cognate tRNAIle and tRNAIle-dependent structural rearrangements consistent with regulation at the level of translation initiation, providing the first biochemical demonstration, to our knowledge, of translational regulation in a T box riboswitch.

U2 - 10.1073/pnas.1424175112

DO - 10.1073/pnas.1424175112

M3 - Journal article

VL - 112

SP - 1113

EP - 1118

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 4

ER -

ID: 368623801