Enzymatic RNA synthesis and RNase P |
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Authors: | Guido Krupp |
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Institution: | (1) Institut für Allgemeine Mikrobiologie, Christian-Albrechts-Universität, Am Botanischen Garten 9, D-24118 Kiel, Germany;(2) Present address: Institut für Hämatopathologie, Christian-Albrechts-Universität, Niemannsweg 11, D-24105 Kiel, Germany |
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Abstract: | TransferRNA recognition was used as leit-motiv in the illustration of possible links between a hypothetical primordial RNA world and the contemporary DNA world. In an RNA world, proto-tRNA could have functioned as replication origin and as primitive telomere. Possibly, this primitive structure is preserved in a universal substrate for modern tRNA-specific enzymes. The combination of acceptor stem and T arm (plus a linker) was finally revealed as sufficient for the recognition by prokaryotic and eukaryotic RNase P, as well as other tRNA enzymes. In modern life forms, a tRNA-like element in viral RNAs still serves as replication origin, and furthermore, the recognition of similar structures as cryptic promoters is universally conserved for template-dependent RNA polymerases. Another common property of modern polymerases is their high, but clearly limited and condition-dependent substrate specificity. Very likely, also substrate recognition by primitive polymerases was not more stringent, and this lead to the ocurrence of mixed nucleic acids as intermediates in the transition from genomic RNA to contemporary genomic DNA.Abbreviations (d)NTP
(deoxy)nucleoside triphosphate
- nt
nucleotide(s) |
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Keywords: | chimeric nucleic acids promoter RNA world T7 RNA polymerase RNase P |
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