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Evolutionary Divergent Suppressor Mutations in Conformational Diseases.

Noel Mesa-Torres¹, Isabel Betancor-Fernández², Elisa Oppici³

¹Department of Physical Chemistry, University of Granada, 18010 Granada, Spain. noelmesatorres@gmail.com.

|July 18, 2018

Summary

Evolutionary divergence from consensus amino acids may increase human protein vulnerability to disease-causing mutations by reducing conformational stability. Mammalian proteins with consensus residues may offer disease suppression, impacting therapeutic strategies.

Keywords:

compensatory mutations conformational diseases disease-mechanisms genotype-phenotype correlations molecular therapies protein stability

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Published on: August 24, 2018

Area of Science:

Protein evolution
Molecular biology
Human genetics

Background:

Destabilizing mutations are rarely tolerated in evolution but cause human conformational diseases.
Human proteins may be more susceptible to disease mutations due to evolutionary divergence from consensus states, impacting conformational stability.

Purpose of the Study:

To extend and refine the hypothesis that evolutionary divergence impacts protein disease vulnerability.
To investigate mechanisms of loss-of-function in diseases involving NQO1 and AGT proteins.
To explore the role of consensus amino acids in disease suppression and phenotypic variability.

Main Methods:

Phylogenetic and structural analyses.
Structure-based energy calculations.
Structure-function studies at molecular and cellular levels.
Focus on mammalian orthologues of NQO1 and AGT proteins.

Main Results:

Divergence from consensus amino acids can decrease protein conformational stability, increasing disease vulnerability.
Loss-of-function mechanisms include enzyme inactivation, accelerated degradation, mistargeting, and aggregation.
Consensus amino acids in mammalian orthologues may act as suppressors of human disease.

Conclusions:

Evolutionary changes in protein sequences influence disease susceptibility.
Understanding these evolutionary dynamics can inform therapeutic approaches for conformational diseases.
Phenotypic variability arises from post-translational modifications and protein quality control, affecting disease models.