Interkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins
Marco Lalle1, Flora Leptourgidou, Serena Camerini
1Department of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità, Rome, Italy.
The 14-3-3 protein from Giardia duodenalis is structurally similar to ancestral 14-3-3ε but functionally distinct. This suggests 14-3-3ε proteins are the evolutionary precursors to other 14-3-3 family members.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Protein Biochemistry
Background:
- 14-3-3 proteins are crucial for eukaryotic cellular functions, with known diversity in higher eukaryotes.
- Information on 14-3-3 proteins primarily comes from higher eukaryotes, leaving lower eukaryotes understudied.
- Sequence conservation suggests a common, ancestral 14-3-3 protein similar to modern 14-3-3ε isoforms.
Purpose of the Study:
- To investigate the structural and functional homology of Giardia duodenalis 14-3-3 (g14-3-3) with Drosophila melanogaster 14-3-3 proteins.
- To test the hypothesis that ancestral 14-3-3 proteins were similar to 14-3-3ε isoforms.
Main Methods:
- Utilized inter-kingdom reciprocal functional complementation assays.
- Employed biochemical methods to assess protein function and homology.
Main Results:
- g14-3-3 exhibits structural homology to Drosophila 14-3-3ε (D14-3-3ε).
- Functionally, g14-3-3 diverges from D14-3-3ε, showing characteristics of other 14-3-3 protein subclasses.
- Giardia's basal position in eukaryotic evolution supports the findings.
Conclusions:
- The study provides evidence that 14-3-3ε isoforms are likely ancestral to other 14-3-3 family members.
- g14-3-3's functional divergence highlights evolutionary adaptation within the 14-3-3 protein family.
- Findings contribute to understanding the evolution of essential cellular proteins in eukaryotes.
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