ArticleNucleic acids research2009
Functional importance of crenarchaea-specific extra-loop revealed by an X-ray structure of a heterotetrameric crenarchaeal splicing endonuclease.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Structural basis of substrate diversity and functional evolution of archaeal RNA-splicing endonucleases.Nucleic acids research · 2025Article
- New insights into RNA processing by the eukaryotic tRNA splicing endonuclease.The Journal of biological chemistry · 2023Review
- Recent insights into the structure, function, and regulation of the eukaryotic transfer RNA splicing endonuclease complex.Wiley interdisciplinary reviews. RNA · 2022Review
- Recent Insights Into the Structure, Function, and Evolution of the RNA-Splicing Endonucleases.Frontiers in genetics · 2019Review
- The RNA-splicing endonuclease from the euryarchaeaon Methanopyrus kandleri is a heterotetramer with constrained substrate specificity.Nucleic acids research · 2018Article
- Circularization restores signal recognition particle RNA functionality in Thermoproteus.eLife · 2015Article
- tRNA gene diversity in the three domains of life.Frontiers in genetics · 2014Review
- Handling tRNA introns, archaeal way and eukaryotic way.Frontiers in genetics · 2014Review
- X-ray structure of the fourth type of archaeal tRNA splicing endonuclease: insights into the evolution of a novel three-unit composition and a unique loop involved in broad substrate specificity.Nucleic acids research · 2012Article
- A novel three-unit tRNA splicing endonuclease found in ultrasmall Archaea possesses broad substrate specificity.Nucleic acids research · 2011Article
- Cleavage of intron from the standard or non-standard position of the precursor tRNA by the splicing endonuclease of Aeropyrum pernix, a hyper-thermophilic Crenarchaeon, involves a novel RNA recognition site in the Crenarchaea specific loop.Nucleic acids research · 2011Article
- Discovery of permuted and recently split transfer RNAs in Archaea.Genome biology · 2011Article
- Transfer RNA processing in archaea: unusual pathways and enzymes.FEBS letters · 2010Review
- Disrupted tRNA gene diversity and possible evolutionary scenarios.Journal of molecular evolution · 2009Article
- Gain and loss of an intron in a protein-coding gene in Archaea: the case of an archaeal RNA pseudouridine synthase gene.BMC evolutionary biology · 2009Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Archaeal splicing endonucleases (EndAs) are currently classified into three groups. Two groups require a single subunit protein to form a homodimer or homotetramer. The third group requires two nonidentical protein components for the activity. To elucidate the molecular architecture of the two-subunit EndA system, we studied a crenarchaeal splicing endonuclease from Pyrobaculum aerophilum. In the present study, we solved a crystal structure of the enzyme at 1.7-A resolution. The enzyme adopts a heterotetrameric form composed of two catalytic and two structural subunits. By connecting the structural and the catalytic subunits of the heterotetrameric EndA, we could convert the enzyme to a homodimer that maintains the broad substrate specificity that is one of the characteristics of heterotetrameric EndA. Meanwhile, a deletion of six amino acids in a Crenarchaea-specific loop abolished the endonuclease activity even on a substrate with canonical BHB motif. These results indicate that the subunit architecture is not a major factor responsible for the difference of substrate specificity between single- and two-subunit EndA systems. Rather, the structural basis for the broad substrate specificity is built into the crenarchaeal splicing endonuclease itself.
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