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Expression, Purification, and Antimicrobial Activity of S100A12
Published on: May 13, 2017
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S100A7/Ran-binding protein 9 coevolution in mammals
Fabio D'Amico1, Francesca Nadalin2, Massimo Libra3
1Department of Biomedical and Biotechnological Sciences, University of Catania, Catania, Italy. f.damico@unict.it.
Immunogenetics
|February 12, 2020
Summary
Coevolutionary analysis reveals a significant link between S100A7 and Ran-binding protein 9 (RanBP9), suggesting amino acid variations impact their interaction and potentially disease pathogenesis.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Immunology
Background:
- S100A7 and Ran-binding protein 9 (RanBP9) are key immune response effectors.
- Functional protein interactions are driven by coevolution.
- Vertebrate coevolution mechanisms between S100A7 and RanBP9 are not well understood.
Purpose of the Study:
- To investigate the coevolutionary mechanisms between S100A7 and RanBP9 in vertebrates.
- To identify potential pathogenic effects arising from variations in S100A7/RanBP9 interactions.
Main Methods:
- Protein coevolution analysis using Mirrortree to calculate correlation coefficients between inter-protein distance matrices.
- Utilized the Blocks in Sequences (BIS2) algorithm via the BIS2Analyzer webserver for coevolutionary analysis, leveraging RanBP9's high vertebrate conservation.
Main Results:
- A moderate overall correlation (R=0.53, p<1e-06) was found between S100A7 and RanBP9 inter-protein distances.
- A significant coevolution cluster was identified between S100A7 and RanBP9 (p<8.10e-05).
Conclusions:
- Coevolutionary analysis supports a functional interaction between S100A7 and RanBP9.
- Amino acid variations may modulate the S100A7/RanBP9 interaction, potentially leading to pathogenic effects.
- Findings may guide future research on S100A7 and RanBP9 functions and drug development for related diseases.
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