Journal
RNA
Volume 16, Issue 1, Pages 79-90Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.1692310
Keywords
box C/D snoRNA; snoRNP; kink-turn; L7Ae/L30 proteins; RNA-protein interaction
Categories
Funding
- NSF [MCB 0543741]
- NIH [GM069699]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM069699] Funding Source: NIH RePORTER
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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 C9/D9 RNP formation or RNA-guided nucleotide modification. L7Ae is still incorporated into the C9/D9 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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