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

. 2018 Mar 28;9:1248. doi: 10.1038/s41467-018-03387-6

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

© The Author(s) 2018

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/.

PMC Copyright notice

Fig. 6 — Protein–protein interactions of AID and R-mutants. a (Left) schemes of AID, AID E58A and fusions thereof indicating additional mutations. (Middle) Relative ability to produce rifampicin resistant (Rif-R) E. coli colonies is shown by means (bars) of median values (dots) from 2 to 4 independent experiments (5 clones/experiment), normalized to the median of AID from each experiment. (Right) Relative CSR capacity of the same proteins expressed in Aicda^−/− mouse B cells. Means (bars) from 4 to 10 independent mice (dots) from 2 to 5 independent experiments are shown, normalized to AID. b Schematic of the AID fusions to BirA* and representative flow cytometric plots for CSR, the proportion of IgG1+ cells in the GFP+ population, in reconstituted Aicda^−/− mouse B cells. APOBEC2 (A2) was used as control. c Representative WB of the AID-BirA* fusions (anti-flag) and biotinylated targets (streptavidin) from reconstituted Aicda^−/− mouse B cells after incubation with biotin. Untransduced cells were used as control (Ctrl). d MA plot showing the fold change in spectral counts (s.c.) as a function of average s.c. of all hits for wt AID versus R-mutants. Red and blue dots represent significant differences identified according to negative binomial distribution by the DESeq2 software. e (Left) Circle plots of BioID signal for selected known AID interacting partners. Circle size indicates relative abundance normalized to the variant with the most s.c. Circle colour represent actual s.c. Scales are shown. f (Left) Broad functional categories of BioID associations found reduced in the R-mutants compared to wt AID. (Right) Circle plots for hits in the indicated categories. g Anti-GFP pull down from whole-cell lysates of AID-deficient CH12 B cells reconstituted with AID variant-GFP fusions. Spt6, Spt5, RNAPII and AID were detected by WB from immunoprecipitates or lysates. Representative of two independent experiments. h Streptavidin pull down of biotinylated proteins from whole-cell lysates of AID-deficient CH12 B cells reconstituted with AID variant-BirA* fusions after 24 h pulse of biotin. Spt6 and AID were detected by WB from either pull downs or lysates. Ratios of Spt6 to AID signal normalized to AID-BirA* are indicated. Representative of two independent experiments. For gel source data, see supplementary Fig. 7