An RNA Polymerase Ribozyme that Synthesizes its Own Ancestor
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ABSTRACT:
PROVIDER: PRJNA595935 | ENA |
REPOSITORIES: ENA
Similar Datasets
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Project description:The RNA-based organisms from which modern life is thought to have descended would have depended on an RNA polymerase ribozyme to copy functional RNA molecules, including copying the polymerase itself. Such a polymerase must have been capable of copying structured RNAs with high efficiency and high fidelity to maintain genetic information across successive generations. Here the class I RNA polymerase ribozyme was evolved in vitro for the ability to synthesize functional ribozymes, resulting in the markedly improved ability to synthesize complex RNAs using nucleoside 5'-triphosphate (NTP) substrates. The polymerase is descended from the class I ligase, which contains the same catalytic core as the polymerase. The class I ligase can be synthesized by the improved polymerase as three separate RNA strands that assemble to form a functional ligase. The polymerase also can synthesize the complement of each of these three strands. Despite this remarkable level of activity, only a very small fraction of the assembled ligases retain catalytic activity due to the presence of disabling mutations. Thus, the fidelity of RNA polymerization should be considered a major impediment to the construction of a self-sustained, RNA-based evolving system. The propagation of heritable information requires both efficient and accurate synthesis of genetic molecules, a requirement relevant to both laboratory systems and the early history of life on Earth.
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Project description:Transcription, the copying of genetic information into RNA, is accomplished by multi-subunit RNA polymerases (msRNAPs) in all living organisms. msRNAPs are highly conserved in evolution and invariantly share a ~400 kDa five-subunit catalytic core1,2. A group of hypothetical single-chain proteins of unknown function, present in various bacteria and bacteriophages, was predicted to be distantly related to msRNAPs, having diverged from them before the Last Universal Common Ancestor3. Here, we studied a ~100 kDa protein, YonO, from this group encoded by the bacteriophage SPβ of Bacillus subtilis. We show that despite homology to only several amino acids of msRNAP, and the absence of most of the conserved domains, YonO is a highly processive and fast DNA-dependent RNA polymerase. Unlike msRNAPs, YonO can start specific transcription on double-stranded DNA without additional factors. We show that YonO is a bona fide RNAP of SPβ bacteriophage that transcribes its late genes. This new class of RNAPs may represent an intermediate step in the evolution of an ancestor of all msRNAPs.
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