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

. 2023 Jun 8;13:9297. doi: 10.1038/s41598-023-35765-6

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

© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

RNA helicase activities of eIF4A mutant proteins containing select natural and non-natural rocaglate-associated aa patterns in a human whole protein background. (A) Helicase V_max of the wild-type human eIF4A1 containing the rocaglate-binding pattern TPFFQI and 17 variants of the human eIF4A1 protein (Table S4), including one expressing the Aglaia sp. aa pattern TPLFQM. All natural and non-natural aa patterns analyzed exhibited V_max within a narrow range, indicating that the helicase activity is maintained. (B) Side-by-side V_max comparison of mutant pairs differing only in the aa residue at position 199 of the eIF4A protein. The two substitutions analyzed, I199V and I199M, are the only natural substitutions at this position revealed by our global eIF4A sequence survey (RF relative fluorescence; error bars indicate mean standard error from three technical replicates; error bars removed in (B) for clarity).