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. 2012 Jan 31;40(10):4666–4680. doi: 10.1093/nar/gks013

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© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Archaeal RPPs affect the RPR's fidelity of processing of a non-consensus substrate. (a) Possible interactions around the cleavage site between nucleotides in typical (consensus) or atypical (non-consensus) pre-tRNAs and the bacterial RPR. (b) Secondary structure of the self-cleaving pre-tRNA^Gln-Mja RPR used in this study. The site of tethering of pre-tRNA^Gln to Mja RPR is depicted. The 5′-aau-3′ spacer is shown in circled lowercase letters. The secondary structure follows conventional representations for all RPRs (100). (c) Rescue of RPR's mis-cleavage by the RPPs. T1, the G ladder generated by RNase T1 digestion of pre-tRNA^Gln. Alk, the ladder obtained from alkaline hydrolysis of pre-tRNA^Gln. Uncleaved pre-tRNA^Gln is shown in lane 1. Cleavage of pre-tRNA^Gln by Pfu RPR, RPR + RPP21•RPP29, RPR + POP5•RPP30 and RPR + both RPP complexes is shown in lanes 2–5, respectively. Lanes 6 and 7 represent uncleaved and self-cleaved pre-tRNA^Gln-Mja RPR, respectively. The cleaved 5′-leader products generated by addition of Mja RPP21•RPP29, POP5•RPP30 and four RPPs to pre-tRNA^Gln-Mja RPR are shown in lanes 8–10. M₊₁, the 5′-leader generated from mis-cleavage between positions +1 and +2 in pre-tRNA^Gln; C₀, the 5′-leader from cleavage at the correct site between positions −1 and +1 in pre-tRNA^Gln.