Determinants of Interaction Specificity of the Bacillus subtilis GlcT Antitermination Protein

Himmel, Sebastian; Zschiedrich, Christopher P.; Becker, Stefan; Hsiao, He-Hsuan; Wolff, Sebastian; Diethmaier, Christine; Urlaub, Henning; Lee, Donghan; Griesinger, Christian; Stülke, Jörg

doi:10.1074/jbc.m112.388850

Cited by 8 publications

(4 citation statements)

References 47 publications

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“…Accordingly, structural investigation on the phosphorylationbased regulation of BglG antiterminators has essentially been performed on phosphomimetic mutants, most often on protein fragments. In vitro phosphorylation of BglG-like antiterminators has been performed (Lindner et al, 1999;Himmel et al, 2012b;Knezevic et al, 2015;Rothe et al, 2012), but the structural consequences of these phosphorylations have usually not been examined. So far, only NMR studies on the PRD1 module of the GlcT antitermination protein have provided direct structural evidence of histidine phosphorylation for this protein family (Himmel et al, 2012b).…”

Section: Discussionmentioning

confidence: 99%

“…In vitro phosphorylation of BglG-like antiterminators has been performed (Lindner et al, 1999;Himmel et al, 2012b;Knezevic et al, 2015;Rothe et al, 2012), but the structural consequences of these phosphorylations have usually not been examined. So far, only NMR studies on the PRD1 module of the GlcT antitermination protein have provided direct structural evidence of histidine phosphorylation for this protein family (Himmel et al, 2012b). In this work, we present the conformational and functional investigation on the activating phosphorylation of full-length LicT.…”

Section: Discussionmentioning

confidence: 99%

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Structural Insights into of the Allosteric Activation of the LicT Antiterminator by PTS-Mediated Phosphorylation

Yang¹,

Padilla²,

Guillen³

et al. 2020

Structure

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LicT belongs to an essential family of bacterial transcriptional antitermination proteins controlling the expression of sugar-metabolizing operons. When activated, they bind to nascent mRNAs, preventing premature arrest of transcription. The RNA binding capacity of the N-terminal domain CAT is controlled by phosphorylations of two homologous regulation modules by the phosphotransferase system (PTS). Previous studies on truncated and mutant proteins provided partial insight into the mechanism of signal transduction between the effector and regulatory modules. We report here the conformational and functional investigation on the allosteric activation of full-length LicT. Combining fluorescence anisotropy and NMR, we find a tight correlation between LicT RNA binding capacity and CAT closure upon PTS-mediated phosphorylation and phosphomimetic mutations. Our study highlights fine structural differences between activation processes. Furthermore, the NMR study of full-length proteins points to the back and forth propagation of structural restraints from the RNA binding to the distal regulatory module.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Structural Insights into of the Allosteric Activation of the LicT Antiterminator by PTS-Mediated Phosphorylation

Yang¹,

Padilla²,

Guillen³

et al. 2020

Structure

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“…LicT interacts with two bulges in the antiterminator and the minor groove of the stem between them (Yang et al, 2002, Figure 8C). In GlcT, arrangement of the PRDs is under selective pressure to ensure a proper regulatory output (Himmel et al, 2012). For SacT, SacY, and LicT, specificity domains were identified that prevent a cross-talk between these systems (Hübner et al, 2011).…”

Section: Rna Binding Proteins Inducing Terminator or Antiterminator Fmentioning

confidence: 99%

Intermolecular Communication in Bacillus subtilis: RNA-RNA, RNA-Protein and Small Protein-Protein Interactions

Haq

Müller

Brantl

2020

Front. Mol. Biosci.

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“…By exploiting the non-destructive and quantitative nature of such NMR measurements, we illustrated another analytical advantage of this approach: The ability to directly follow PTM reactions in a time-resolved fashion in order to deduce site-specific modification rates [97,98]. Indeed, protein phosphorylation studies by time-resolved NMR spectroscopy became very popular and proved essential for delineating mechanistic insights into diverse sets of signaling reactions [99,100,101,102,103,104,105,106,107,108,109,110,111,112,113,114,115,116,117,118,119,120,121,122,123,124,125,126,127,128,129,130,131,132,133,134,135].…”

Section: Detecting Post-translational Protein Modifications By Nmrmentioning

confidence: 99%

Quo Vadis Biomolecular NMR Spectroscopy?

Selenko

2019

IJMS

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In-cell nuclear magnetic resonance (NMR) spectroscopy offers the possibility to study proteins and other biomolecules at atomic resolution directly in cells. As such, it provides compelling means to complement existing tools in cellular structural biology. Given the dominance of electron microscopy (EM)-based methods in current structure determination routines, I share my personal view about the role of biomolecular NMR spectroscopy in the aftermath of the revolution in resolution. Specifically, I focus on spin-off applications that in-cell NMR has helped to develop and how they may provide broader and more generally applicable routes for future NMR investigations. I discuss the use of ‘static’ and time-resolved solution NMR spectroscopy to detect post-translational protein modifications (PTMs) and to investigate structural consequences that occur in their response. I argue that available examples vindicate the need for collective and systematic efforts to determine post-translationally modified protein structures in the future. Furthermore, I explain my reasoning behind a Quinary Structure Assessment (QSA) initiative to interrogate cellular effects on protein dynamics and transient interactions present in physiological environments.

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Determinants of Interaction Specificity of the Bacillus subtilis GlcT Antitermination Protein

Cited by 8 publications

References 47 publications

Structural Insights into of the Allosteric Activation of the LicT Antiterminator by PTS-Mediated Phosphorylation

Structural Insights into of the Allosteric Activation of the LicT Antiterminator by PTS-Mediated Phosphorylation

Intermolecular Communication in Bacillus subtilis: RNA-RNA, RNA-Protein and Small Protein-Protein Interactions

Quo Vadis Biomolecular NMR Spectroscopy?

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