The interaction strength of an intrinsically disordered protein domain with its binding partner is little affected by very different cosolutes

Schnatwinkel, Jan; Herrmann, Christian

doi:10.1039/d0cp03040f

Search citation statements

Order By: Relevance

Paper Sections

Select...

Solution-space Scanning Reveals a Link Between Hidden Structural Preferences And Sensitivity To Solution Composition1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2021

Publication Types

Select...

Preprint1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

(1 citation statement)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S5). This is in line with other observations that show both sensitivity 5,8,63,64 and insensitivity 65,66 of IDP function to different solution environments. In our constructs, the most prominent changes were seen in E1A, which displayed very strong deviations from GS-repeat homopolymers both in and and in its response to solute changes, and p53 NTAD, which 𝑅 𝑒 𝑎𝑝𝑝 𝑅 𝑔 shows the closest behavior to a GS homopolymer in each of these metrics (Fig.…”

Section: Solution-space Scanning Reveals a Link Between Hidden Structural Preferences And Sensitivity To Solution Compositionsupporting

confidence: 93%

Structural biases in disordered proteins are prevalent in the cell

Moses

Guadalupe

et al. 2021

Preprint

View full text Add to dashboard Cite

Intrinsically disordered protein regions (IDRs) are ubiquitous in all proteomes and essential to cellular function. Unlike folded domains, IDRs exist in an ensemble of rapidly changing conformations. The sequence-encoded structural biases in IDR ensembles are important for function, but are difficult to resolve. Here, we reveal hidden structural preferences in IDR ensembles in vitro with two orthogonal structural methods (SAXS and FRET), and demonstrate that these structural preferences persist in cells using live cell microscopy. Importantly, we demonstrate that some IDRs have structural preferences that can adaptively respond to even mild intracellular environment changes, while other IDRs may display a remarkable structural resilience. We propose that the ability to sense and respond to changes in cellular physicochemical composition, or to resist such changes, is a sequence-dependent property of IDRs in organisms across all kingdoms of life.

show abstract