Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae
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2000-05
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L Lindahl, et.al, Functional equivalence of hairpins in the RNA subunits of RNase MRP and RNase P in Saccharomyces cerevisiae, RNA. 2000 May; 6(5): 653–658, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1369945/
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Abstract
RNase MRP and RNase P are both ribonucleoprotein enzymes performing endonucleolytic cleavage of RNA. RNase
MRP cleaves at a specific site in the precursor-rRNA transcript to initiate processing of the 5.8S rRNA. RNase P
cleaves precursor tRNAs to create the 59 end of the mature tRNAs. In spite of their different specificities, the two
RNases have significant structural similarities. For example, the two enzymes in Saccharomyces cerevisiae share
eight protein subunits; only one protein is unique to each enzyme. The RNA components of the two nucleases also
show striking secondary-structure similarity. To begin to characterize the role of the RNA subunits in enzyme function
and substrate specificity, we swapped two hairpin structures (MRP3 and P3) between RNase MRP RNA and RNase P
RNA of S. cerevisiae. The hairpins in the two enzymes could be exchanged without loss of function or specificity. On
the other hand, when the MRP3 hairpin in RNase MRP of S. cerevisiae was replaced with the corresponding hairpin
from the RNA of Schizosaccharomyces pombe or human RNase MRP, no functional enzyme was assembled. We
propose that the MRP3 and P3 hairpins in S. cerevisiae perform similar functions and have coevolved to maintain
common features that are different from those of MRP3 and P3 hairpins in other species.