ArticleComputational and structural biotechnology journal2021
CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- The First Poly(A) Polymerase fromInternational journal of molecular sciences · 2026Article
- Two complementingRNA biology · 2025Article
- Crystal structure of the CCA-adding enzyme fromJournal of structural biology: X · 2025Article
- Genomic analyses reveal a low-temperature adapted clade in Halorubrum, a widespread haloarchaeon across global hypersaline environments.BMC genomics · 2023Article
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7 authors at 2 institutions in 2 countries.
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Abstract
CCA-adding enzymes are highly specific RNA polymerases that add and maintain the sequence C-C-A at tRNA 3'-ends. Recently, we could reveal that cold adaptation of such a polymerase is not only achieved at the expense of enzyme stability, but also at the cost of polymerization fidelity. Enzymes from psychrophilic organisms usually show an increased structural flexibility to enable catalysis at low temperatures. Here, polymerases face a dilemma, as there is a discrepancy between the need for a tightly controlled flexibility during polymerization and an increased flexibility as strategy for cold adaptation. Based on structural and biochemical analyses, we contribute to clarify the cold adaptation strategy of the psychrophilic CCA-adding enzyme from
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