Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p
Key result
Human RNase L and yeast Ire1p showed mutually exclusive RNA substrate specificity and partially overlapping requirements for conserved amino acid residues in their nuclease domains.
Population
Wild-type and mutant forms of human RNase L and yeast Ire1p
Design
Preclinical
Authors
Discussion
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Member takes
Implication
Species-specific nuclease differences caution against yeast-to-human extrapolation; leaves open RNase L targeting in cardiovascular inflammation research.
Structured PICO
P
Population
Wild-type and mutant forms of human RNase L and yeast Ire1p
I
Intervention
Comparative functional analysis of molecular properties
O
Outcome
RNA substrate specificity and requirements for phylogenetically conserved amino acid residues in nuclease domains
Comparative analysis of human RNase L and yeast Ire1p reveals mutually exclusive RNA substrate specificity and assigns novel roles for ankyrin repeats and kinase-like domains in RNase L.
Cite This Study
Dong et al. (2001) studied this question. Wild-type and mutant forms of human RNase L and yeast Ire1p was evaluated on RNA substrate specificity and requirements for phylogenetically conserved amino acid residues. Human RNase L and yeast Ire1p showed mutually exclusive RNA substrate specificity and partially overlapping requirements for conserved amino acid residues in their nuclease domains.