RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme - PubMed (original) (raw)
. 2008 Oct 31;135(3):462-74.
doi: 10.1016/j.cell.2008.09.013.
Affiliations
- PMID: 18984158
- DOI: 10.1016/j.cell.2008.09.013
Free article
RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
Johann Holzmann et al. Cell. 2008.
Free article
Abstract
tRNAs are synthesized as immature precursors, and on their way to functional maturity, extra nucleotides at their 5' ends are removed by an endonuclease called RNase P. All RNase P enzymes characterized so far are composed of an RNA plus one or more proteins, and tRNA 5' end maturation is considered a universal ribozyme-catalyzed process. Using a combinatorial purification/proteomics approach, we identified the components of human mitochondrial RNase P and reconstituted the enzymatic activity from three recombinant proteins. We thereby demonstrate that human mitochondrial RNase P is a protein enzyme that does not require a trans-acting RNA component for catalysis. Moreover, the mitochondrial enzyme turns out to be an unexpected type of patchwork enzyme, composed of a tRNA methyltransferase, a short-chain dehydrogenase/reductase-family member, and a protein of hitherto unknown functional and evolutionary origin, possibly representing the enzyme's metallonuclease moiety. Apparently, animal mitochondria lost the seemingly ubiquitous RNA world remnant after reinventing RNase P from preexisting components.
Comment in
- A protein-only RNase P in human mitochondria.
Walker SC, Engelke DR. Walker SC, et al. Cell. 2008 Oct 31;135(3):412-4. doi: 10.1016/j.cell.2008.10.010. Cell. 2008. PMID: 18984152 Free PMC article.
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