Multisite Phosphorylation and Binding Alter Conformational Dynamics of the 4E-BP2 Protein Article Swipe
Spencer Smyth
,
Zhenfu Zhang
,
Alaji Bah
,
Thomas E. Tsangaris
,
Jennifer E. Dawson
,
Julie D. Forman‐Kay
,
Claudiu C. Gradinaru
·
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.01.14.476386
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1101/2022.01.14.476386
Intrinsically disordered proteins (IDPs) play critical roles in regulatory protein interactions, but detailed structural/dynamics characterization of their ensembles remain challenging, both in isolation and they form dynamic ‘fuzzy’ complexes. Such is the case for mRNA cap-dependent translation initiation, which is regulated by the interaction of the predominantly folded eukaryotic initiation factor 4E (eIF4E) with the intrinsically disordered eIF4E binding proteins (4E-BPs) in a phosphorylation-dependent manner. Single-molecule Förster resonance energy transfer showed that the conformational changes of 4E-BP2 induced by binding to eIF4E are non-uniform along the sequence; while a central region containing both motifs that bind to eIF4E expands and becomes stiffer, the C-terminal region is less affected. Fluorescence anisotropy decay revealed a nonuniform segmental flexibility around six different labelling sites along the chain. Dynamic quenching of these fluorescent probes by intrinsic aromatic residues measured via fluorescence correlation spectroscopy report on transient intra- and inter-molecular contacts on ns-μs timescales. Upon hyperphosphorylation, which induces folding of ~40 residues in 4E-BP2, the quenching rates decreased at most labelling sites. The chain dynamics around sites in the C-terminal region far away from the two binding motifs significantly increased upon binding to eIF4E, suggesting that this region is also involved in the highly dynamic 4E-BP2:eIF4E complex. Our time-resolved fluorescence data paint a sequence-level rigidity map of three states of 4E-BP2 differing in phosphorylation or binding status and distinguish regions that form contacts with eIF4E. This study adds complementary structural and dynamics information to recent studies of 4E-BP2, and it constitutes an important step towards a mechanistic understanding of this important IDP via integrative modelling.
Related Topics
Concepts
Biophysics
Intrinsically disordered proteins
Chemistry
Fluorescence anisotropy
Binding site
Phosphorylation
Quenching (fluorescence)
Förster resonance energy transfer
EIF4E
Crystallography
Folding (DSP implementation)
Fluorescence
Biochemistry
Biology
Translation (biology)
Messenger RNA
Physics
Electrical engineering
Gene
Membrane
Quantum mechanics
Engineering
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2022.01.14.476386
- https://www.biorxiv.org/content/biorxiv/early/2022/05/20/2022.01.14.476386.full.pdf
- OA Status
- green
- References
- 60
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4205972789
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4205972789Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2022.01.14.476386Digital Object Identifier
- Title
-
Multisite Phosphorylation and Binding Alter Conformational Dynamics of the 4E-BP2 ProteinWork title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2022Year of publication
- Publication date
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2022-01-15Full publication date if available
- Authors
-
Spencer Smyth, Zhenfu Zhang, Alaji Bah, Thomas E. Tsangaris, Jennifer E. Dawson, Julie D. Forman‐Kay, Claudiu C. GradinaruList of authors in order
- Landing page
-
https://doi.org/10.1101/2022.01.14.476386Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2022/05/20/2022.01.14.476386.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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-
greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2022/05/20/2022.01.14.476386.full.pdfDirect OA link when available
- Concepts
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Biophysics, Intrinsically disordered proteins, Chemistry, Fluorescence anisotropy, Binding site, Phosphorylation, Quenching (fluorescence), Förster resonance energy transfer, EIF4E, Crystallography, Folding (DSP implementation), Fluorescence, Biochemistry, Biology, Translation (biology), Messenger RNA, Physics, Electrical engineering, Gene, Membrane, Quantum mechanics, EngineeringTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
- References (count)
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60Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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