Interkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins.
Interkingdom complementation reveals structural conservation and functional divergence of 14-3-3 proteins.
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王国间互补揭示了 14-3-3 蛋白的结构保守性和功能差异。
DOI:
10.1371/journal.pone.0078090
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Skoulakis EM
中科院分区:
文献类型:
--
作者:
Lalle M;Leptourgidou F;Camerini S;Pozio E;Skoulakis EM
The 14-3-3s are small acidic cytosolic proteins that interact with multiple clients and participate in essential cellular functions in all eukaryotes. Available structural and functional information about 14-3-3s is largely derived from higher eukaryotes, which contain multiple members of this protein family suggesting functional specialization. The exceptional sequence conservation among 14-3-3 family members from diverse species suggests a common ancestor for 14-3-3s, proposed to have been similar to modern 14-3-3ε isoforms. Structural features of the sole family member from the protozoan Giardia duodenalis (g14-3-3), are consistent with this hypothesis, but whether g14-3-3 is functionally homologous to the epsilon isoforms is unknown. We use inter-kingdom reciprocal functional complementation and biochemical methods to determine whether g14-3-3 is structurally and functionally homologous with members of the two 14-3-3 conservation groups of the metazoan Drosophila melanogaster. Our results indicate that although g14-3-3 is structurally homologous to D14-3-3ε, functionally it diverges presenting characteristics of other 14-3-3s. Given the basal position of Giardia in eukaryotic evolution, this finding is consistent with the hypothesis that 14-3-3ε isoforms are ancestral to other family members.
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影响因子:
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通讯作者:
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通讯作者:
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