Related Experiment Video
Updated: Jun 16, 2026
Protein-tRNA Agarose Gel Retardation Assays for the Analysis of the N6-threonylcarbamoyladenosine TcdA Function
Published on: June 21, 2017
Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose
Mirjam Metzner1, Wolfgang Schuh, Edith Roth
1Nikolaus-Fiebiger Center, Department of Internal Medicine III, Division of Molecular Immunology, University of Erlangen-Nürnberg, Erlangen, Germany. mirjam.metzner@ucsf.edu
Background:
Activation-induced cytidine deaminase (AID) is a B-cell-specific DNA mutator that plays a key role in the formation of the secondary antibody repertoire in germinal center B cells. In the search for binding partners, protein coimmunoprecipitation assays are often performed, generally with agarose beads.
Methodology/Principal Findings:
We found that, regardless of whether cell lysates containing exogenous or endogenous AID were examined, one of two mouse AID forms bound to agarose alone.
Conclusions/Significance:
These binding characteristics may be due to the known post-translational modifications of AID; they may also need to be considered in coimmunoprecipitation experiments to avoid false-positive results.
