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Deciphering Divergent Trypanosomatid Nuclear Complexes by Analyzing Interactomic Datasets with AlphaFold2 and Genetic
Elvio Rodriguez Araya1,2, Marcelo L Merli1,2, Pamela Cribb1,2
1Instituto de Biología Molecular y Celular de Rosario, CONICET, Suipacha 590, CP2000 Rosario, Argentina.
ACS Infectious Diseases
|May 11, 2023
Summary
We identified novel protein complexes in trypanosomatids using AlphaFold2, revealing new insights into acetylation signaling and potential therapeutic targets. This approach overcomes challenges posed by divergent protein sequences in early-branching organisms.
Area of Science:
- Molecular Biology
- Structural Biology
- Eukaryotic Cell Biology
Background:
- Acetylation signaling pathways in trypanosomatids are poorly understood due to highly divergent protein sequences.
- MORF4 related gene (MRG) domain-containing proteins are typically involved in histone acetyltransferase/deacetylase complexes.
Purpose of the Study:
- To identify and characterize protein complexes in trypanosomatids using interactomic data and AlphaFold2 (AF2)-multimer.
- To investigate the role of MRG domain-containing proteins in trypanosomatid biology.
Main Methods:
- Utilized interactomic datasets and AlphaFold2 (AF2)-multimer for protein interaction prediction.
- Validated predictions using yeast two and three-hybrid assays.
- Employed molecular dynamics simulations to study protein conformational changes.
Main Results:
- Identified a conserved trimeric complex, TcTINTIN, orthologous to human and yeast TINTIN complexes.
- Discovered a novel trypanosomatid-specific trimeric complex involving an MRG domain.
- Revealed a unique MRG domain interaction mode with two binding proteins.
- Identified TcMRGBP as a key component of TcTINTIN, not discoverable by homology methods.
Conclusions:
- AlphaFold2-processed interactomic data is effective for identifying protein complexes in deeply branched eukaryotes.
- MRG domain-containing proteins play a crucial role in forming complexes in trypanosomatids.
- Findings offer insights into acetylation signaling and potential therapeutic targets in trypanosomatids.
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