ArticleMolecular biology and evolution2020
The Universally Conserved Residues Are Not Universally Required for Stable Protein Expression or Functions of Cryptochromes.
Article in Molecular biology and evolution, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 12 citations in OpenAlex.
- A structural view of plant CRY2 photoactivation and inactivation.Nature structural & molecular biology · 2020Article
- Mechanisms of Cryptochrome-Mediated Photoresponses in Plants.Annual review of plant biology · 2020Article
- Photooligomerization Determines Photosensitivity and Photoreactivity of Plant Cryptochromes.Molecular plant · 2020Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Universally conserved residues (UCRs) are invariable amino acids evolutionarily conserved among members of a protein family across diverse kingdoms of life. UCRs are considered important for stability and/or function of protein families, but it has not been experimentally examined systematically. Cryptochromes are photoreceptors in plants or light-independent components of the circadian clocks in mammals. We experimentally analyzed 51 UCRs of Arabidopsis cryptochrome 2 (CRY2) that are universally conserved in eukaryotic cryptochromes from Arabidopsis to human. Surprisingly, we found that UCRs required for stable protein expression of CRY2 in plants are not similarly required for stable protein expression of human hCRY1 in human cells. Moreover, 74% of the stably expressed CRY2 proteins mutated in UCRs retained wild-type-like activities for at least one photoresponses analyzed. Our finding suggests that the evolutionary mechanisms underlying conservation of UCRs or that distinguish UCRs from non-UCRs determining the same functions of individual cryptochromes remain to be investigated.
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