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PreprintCited by 1RNA Research and SplicingProtein Structure and DynamicsRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates

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Chris Ng, Tin Long, Hoare, Mateo P., Maristany, M. Julia, Wilde, Ellis J., Sneideris, Tomas, Huertas, Jan, Agbetiameh, Belinda K., Furukawa, Mona, Joseph, Jerelle A., Knowles, Tuomas P.J., Collepardo-Guevara, Rosana, Itzhaki, Laura S., Kumita, Janet R.·2024·bioRxiv (Cold Spring Harbor Laboratory)
DOI 10.1101/2024.04.16.589709

Preprint — published as 10.1039/d5sc00903k

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Abstract

The cell’s ability to rapidly partition biomolecules into biomolecular condensates is linked to a diverse range of cellular functions. Understanding how the structural attributes of biomolecular condensates are linked with their biological roles can be facilitated by the development synthetic condensate systems that can be manipulated in a controllable and predictable way. Here, we design and characterise a tuneable synthetic biomolecular condensate platform fusing modular consensus-designed tetratricopeptide repeat (CTPR) proteins to intrinsically-disordered domains. Trends between the CTPR structural attributes and condensate propensity were recapitulated across different experimental conditions and by in silico modelling, demonstrating that the CTPR domain can systematically affect the condensates in a predictable manner. Moreover, we show that incorporating short binding motifs into the CTPR domain results in specific target-protein recruitment into the condensates. Our model system can be rationally designed in a versatile manner to both tune condensate propensity and endow the condensates with new functions.

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Metadata

Authors
Chris Ng, T. L., Hoare, M. P., Maristany, M. J., Wilde, E. J., Sneideris, T., Huertas, J., Agbetiameh, B. K., Furukawa, M., Joseph, J. A., Knowles, T. P. J., Collepardo-Guevara, R., Itzhaki, L. S., & Kumita, J. R.
Affiliations
  • University of Cambridge (GB)
  • Princeton University (US)
Corresponding author
Kumita, Janet R.
ORCID
Venue
bioRxiv (Cold Spring Harbor Laboratory)
Publisher
openRxiv
Published
2024-04-20
DOI
10.1101/2024.04.16.589709
OpenAlex
W4394988291
Cited by
1
References
1
Citations by year
2025: 1
Type
posted content
Language
en
Open access
Licence
Locations
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Apollo (University of Cambridge) (submittedVersion, cc-by)
Funders
  • European Commission (101023060)
  • Engineering and Physical Sciences Research Council (EP/X02332X/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
biomolecular condensates, tetratricopeptide repeat proteins, intrinsically disordered regions, in silico modeling, liquid-liquid phase separation

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