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Title: Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly

Abstract

A T-box regulator or riboswitch actively monitors the levels of charged/uncharged tRNA and participates in amino acid homeostasis by regulating genes involved in their utilization or biosynthesis. It has an aptamer domain for cognate tRNA recognition and an expression platform to sense the charge state and modulate gene expression. These two conserved domains are connected by a variable linker that harbors additional secondary structural elements, such as Stem III. The structural basis for specific tRNA binding is known, but the structural basis for charge sensing and the role of other elements remains elusive. To gain new structural insights on the T-box mechanism, a molecular envelope was calculated from small angle X-ray scattering data for the Bacillus subtilis glyQS T-box riboswitch in complex with an uncharged tRNAGly. A structural model of an antiterminated glyQS T-box in complex with its cognate tRNAGly was derived based on the molecular envelope. It shows the location and relative orientation of various secondary structural elements. The model was validated by comparing the envelopes of the wild-type complex and two variants. The structural model suggests that in addition to a possible regulatory role, Stem III could aid in preferential stabilization of the T-box anti-terminated state allowing read-throughmore » of regulated genes.« less

Authors:
 [1];  [1]
  1. Northwestern Univ., Evanston, IL (United States). Dept. of Molecular Biosciences
Publication Date:
Research Org.:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
OSTI Identifier:
1625566
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Nucleic Acids Research
Additional Journal Information:
Journal Volume: 45; Journal Issue: 13; Journal ID: ISSN 0305-1048
Publisher:
Oxford University Press
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Biochemistry & Molecular Biology

Citation Formats

Chetnani, Bhaskar, and Mondragón, Alfonso. Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly. United States: N. p., 2017. Web. doi:10.1093/nar/gkx451.
Chetnani, Bhaskar, & Mondragón, Alfonso. Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly. United States. https://doi.org/10.1093/nar/gkx451
Chetnani, Bhaskar, and Mondragón, Alfonso. Mon . "Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly". United States. https://doi.org/10.1093/nar/gkx451. https://www.osti.gov/servlets/purl/1625566.
@article{osti_1625566,
title = {Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly},
author = {Chetnani, Bhaskar and Mondragón, Alfonso},
abstractNote = {A T-box regulator or riboswitch actively monitors the levels of charged/uncharged tRNA and participates in amino acid homeostasis by regulating genes involved in their utilization or biosynthesis. It has an aptamer domain for cognate tRNA recognition and an expression platform to sense the charge state and modulate gene expression. These two conserved domains are connected by a variable linker that harbors additional secondary structural elements, such as Stem III. The structural basis for specific tRNA binding is known, but the structural basis for charge sensing and the role of other elements remains elusive. To gain new structural insights on the T-box mechanism, a molecular envelope was calculated from small angle X-ray scattering data for the Bacillus subtilis glyQS T-box riboswitch in complex with an uncharged tRNAGly. A structural model of an antiterminated glyQS T-box in complex with its cognate tRNAGly was derived based on the molecular envelope. It shows the location and relative orientation of various secondary structural elements. The model was validated by comparing the envelopes of the wild-type complex and two variants. The structural model suggests that in addition to a possible regulatory role, Stem III could aid in preferential stabilization of the T-box anti-terminated state allowing read-through of regulated genes.},
doi = {10.1093/nar/gkx451},
journal = {Nucleic Acids Research},
number = 13,
volume = 45,
place = {United States},
year = {Mon May 22 00:00:00 EDT 2017},
month = {Mon May 22 00:00:00 EDT 2017}
}

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