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

. 2020 May 4;48(10):5511–5526. doi: 10.1093/nar/gkaa211

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

© The Author(s) 2020. 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 4. — In vitro methylation of Alba3 and RBP16 by PRMT7. (A) Recombinant His-PRMT7 was tested for methyltransferase activity in vitro in the presence of radioactive methyl donor S-adenosyl methionine, human histone H4 as (1 μg) a canonical RGG-containing PRMT substrate (black arrow) and a Leishmania braziliensis protein rich in arginines but devoid of RGG motifs as a negative control (LbrPGF2S). (B) Purified His-tagged PRMT7 putative substrates Alba3^WT, RBP16^WT and RGG-deficient Alba3^ΔRGG were tested, as well as LbrPGF2S^WT. PRMT7 E202 residue in the double E loop motif was mutated to K or Q to generate catalytically-inactive mutants. (C) RNA-binding proteins Alba3^WT and RBP16 are arginine methylated by PRMT7 in vitro, while Alba3^ΔRGG and LbrPGF2S^WT are not. (D) In vitro methylation of target RBPs by PRMT7 is disrupted by mutating residue E202 (PRMT7^E202K and PRMT7^E202Q). Coomassies demonstrate relative loading.