Amino acid repeat mosaics shape protein functional landscape
Anjali Kumari SinghiD, Anurag BabuiD, Adhithya Subramanian GopalakrishnaniD, Nagashree RachoteiD, Vaidehi SharmaiD, Sourav GanguliiD, Keertana Sai KappagantulaiD, Harikrishnan RamadasaniD, Palak Shukla, Arunkumar DhayalaniD, Pavithra Lakshminarasimhan ChavaliiD, Sreenivas ChavaliiD
Abstract
How combinations of functional units such as repeats and motifs within disordered regions influence protein functions remains poorly understood. Here, we investigate how co-occurring amino acid homorepeats of different types within the same protein (HR-mosaics) shape molecular outcomes. Using a novel evolutionary co-occurrence metric, human HR-mosaics were classified as segregated (each HR independently influences distinct outcomes), concerted-disjunct (both HRs jointly shape protein functionality without modulating each other), or concerted-conjunct (both HRs affect functionality through mutual influence). Molecular studies of naturally occurring polyGly-polyPro mosaic in DDX17 and chimeric mosaics of polyAla and polyHis demonstrate that HR-mosaics influence protein abundance, localisation, mobility and interaction landscape. Segregated HR-mosaics expand functional space, concerted-disjunct additionally confer biological context, and concerted-conjunct mosaics further enable rheostatic regulation between HRs. These design principles underscore amino acid type, length and relative positioning of HRs as central architects of HR-mosaic functionality, with implications in protein design and engineering and understanding repeat-associated pathologies.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Size and structure of the sequence space of repeat proteins
J. Marchi, E. A. Galpern, … T. Mora·bioRxiv·May 16, 2019
- Proteins with amino acid repeats constitute rapidly evolvable and human-specific essentialome
Anjali Kumari Singh, Ishita Amar, … Sreenivas Chavali·Cell ReportsPeer-reviewed·Jul 1, 2023
- Phase separation driven by interchangeable properties in the intrinsically disordered regions of protein paralogs
S.-H. Chiu, W.-L. Ho, … J.-r. Huang·bioRxiv·Jan 19, 2022
- From Sequence to Function: Coevolving Amino Acids Encode Structural and Functional Domains
Daniele Granata, Luca Ponzoni, … Vincenzo Carnevale·Proceedings of the National Academy of SciencesPeer-reviewed·Nov 28, 2017
- RepeatParam: Algorithm for Parameterising Repeat Proteins and Analysis of Repeat Protein Architectures
Daniella Pretorius, James W. Murray·bioRxiv·Sep 5, 2024
- Inferring amino acid interactions underlying protein function
V. H. Salinas, R. Ranganathan·bioRxiv·Nov 7, 2017