Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2014 Aug 20;42(16):10711–10719. doi: 10.1093/nar/gku768

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 2. — The influence of the PPP-context on efficiency of the stalling. (A) Schematic representations of chimeras constructed between NlpD and LepA with sites of stalling observed in the absence of EF-P (green and blue arrows) or in the absence of the amino acid glutamine (purple arrow). (B,C) Autoradiograms of SDS-PAGE of in vitro translation reactions of (B) wild-type NlpD, _5:1NlpD and _10:1NlpD chimeras and (C) wild-type LepA, _5:1LepA and _10:1LepA chimeras. The position of the FL protein and peptidyl-tRNA is indicated with black and blue arrows, respectively. In (B) and (C), the normalized values for the FL product are indicated for each respective lane with wild-type FL product for NlpD and LepA assigned as 1. (D) Toeprinting analyses of ribosome stalling during translation of NlpD chimeras. Stalling at peptidyl-Pro55-Pro56-tRNA in the P-site and Pro57-tRNA in the A-site (blue arrow) and with pep-PPP-tRNA in the P-site and Lys58-tRNA in the A-site (green arrow) is also shown in (A). The lack of glutamine arrests ribosomes at Q66 (violet arrow). Stalling efficiency is calculated as a percentage of stalling at PP/P and PPP/K relative to summed up intensities of PP/P, PPP/K and Q. All reactions were performed in the absence (−) and presence (+) of active EF-P.