ArticleExtremophiles : life under extreme conditions2019
Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site.
Article in Extremophiles : life under extreme conditions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Structural Basis for the Propagation of Homing Endonuclease-Associated Inteins.Frontiers in molecular biosciences · 2022Article
- Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins.Microorganisms · 2021Article
- An alternative domain-swapped structure of the Pyrococcus horikoshii PolII mini-intein.Scientific reports · 2021Article
- The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms.International journal of molecular sciences · 2020Article
- Protein Splicing Activity of theBiochemistry · 2020Article
- Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein.Biochemistry · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Self-splicing inteins are mobile genetic elements invading host genes via nested homing endonuclease (HEN) domains. All HEN domains residing within inteins are inserted at a highly conserved insertion site. A purifying selection mechanism directing the location of the HEN insertion site has not yet been identified. In this work, we solved the three-dimensional crystal structures of two inteins inserted in the cell division control protein 21 of the hyperthermophilic archaea Pyrococcus abyssi and Pyrococcus horikoshii. A comparison between the structures provides the structural basis for the thermo-stabilization mechanism of inteins that have lost the HEN domain during evolution. The presence of an entire extein domain in the intein structure from Pyrococcus horikoshii suggests the selection mechanism for the highly conserved HEN insertion point.
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