ArticleRNA (New York, N.Y.)2010
Signature amino acids enable the archaeal L7Ae box C/D RNP core protein to recognize and bind the K-loop RNA motif.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- Directed evolution of orthogonal RNA-RBP pairs through library-vs-library in vitro selection.Nucleic acids research · 2022Article
- Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites.Scientific reports · 2021Article
- H/ACA Small Ribonucleoproteins: Structural and Functional Comparison Between Archaea and Eukaryotes.Frontiers in microbiology · 2021Review
- Conservation of Archaeal C/D Box sRNA-Guided RNA Modifications.Frontiers in microbiology · 2021Review
- Article
- Article
- A nucleolar AAA-NTPase is required for parasite division.Molecular microbiology · 2013Article
- Quantitative and simultaneous translational control of distinct mammalian mRNAs.Nucleic acids research · 2013Article
- Identification of nucleotides and amino acids that mediate the interaction between ribosomal protein L30 and the SECIS element.BMC molecular biology · 2013Article
- Ribonucleoproteins in archaeal pre-rRNA processing and modification.Archaea (Vancouver, B.C.) · 2013Review
- YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops.RNA (New York, N.Y.) · 2012Article
- Feedback control of protein expression in mammalian cells by tunable synthetic translational inhibition.ACS synthetic biology · 2012Article
- Article
- Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface.Journal of molecular biology · 2011Article
- Box C/D snoRNP catalysed methylation is aided by additional pre-rRNA base-pairing.The EMBO journal · 2011Article
- The spatial-functional coupling of box C/D and C'/D' RNPs is an evolutionarily conserved feature of the eukaryotic box C/D snoRNP nucleotide modification complex.Molecular and cellular biology · 2011Article
- Dissecting the role of conserved box C/D sRNA sequences in di-sRNP assembly and function.Nucleic acids research · 2010Article
- Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle.Molecular cell · 2010Article
- Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The archaeal L7Ae and eukaryotic 15.5kD protein homologs are members of the L7Ae/15.5kD protein family that characteristically recognize K-turn motifs found in both archaeal and eukaryotic RNAs. In Archaea, the L7Ae protein uniquely binds the K-loop motif found in box C/D and H/ACA sRNAs, whereas the eukaryotic 15.5kD homolog is unable to recognize this variant K-turn RNA. Comparative sequence and structural analyses, coupled with amino acid replacement experiments, have demonstrated that five amino acids enable the archaeal L7Ae core protein to recognize and bind the K-loop motif. These signature residues are highly conserved in the archaeal L7Ae and eukaryotic 15.5kD homologs, but differ between the two domains of life. Interestingly, loss of K-loop binding by archaeal L7Ae does not disrupt C'/D' RNP formation or RNA-guided nucleotide modification. L7Ae is still incorporated into the C'/D' RNP despite its inability to bind the K-loop, thus indicating the importance of protein-protein interactions for RNP assembly and function. Finally, these five signature amino acids are distinct for each of the L7Ae/L30 family members, suggesting an evolutionary continuum of these RNA-binding proteins for recognition of the various K-turn motifs contained in their cognate RNAs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.