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. 2017 Aug 29;7:9580. doi: 10.1038/s41598-017-10057-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Heterologous expression of Dm eIF5A allows translation of the yeast polyPro formin BNI1 in Sc eIF5A-depleted cells. (A) Schematic diagrams with domains of HA genomic-tagged Bni1. The FH domains, the polyPro stretches with the number of consecutive prolines (red) and the position of the first amino acid of each domain/stretch (below) are indicated. (B) Western blot for Bni1-HA (anti-HA) and Hxk2 expression in wild-type and tif51A-1 cells at 25 or 37 °C at the indicated times. (C) Translation efficiency of BNI1-HA relative to that of HXK2 in wild-type and tif51A-1 cells. Protein/mRNA ratios for Bni1 and Hxk2 were calculated by Western and qRT-PCR from same samples. Translation efficiency of BNI1-HA was calculated relative to translation efficiency of HXK2 and represented as a fraction against 25 °C for each strain and from two independent experiments. Data are represented as mean ± SD. Two-tailed student’s t-test analysis: *p < 0.05, **p < 0.01.