Two Forms of Activation-Induced Cytidine Deaminase Differing in Their Ability to Bind Agarose |
| |
| Authors: | Mirjam Metzner Wolfgang Schuh Edith Roth Hans-Martin J?ck Matthias Wabl |
| |
| Institution: | 1. Nikolaus-Fiebiger Center, Department of Internal Medicine III, Division of Molecular Immunology, University of Erlangen-Nürnberg, Erlangen, Germany.; 2. Department of Microbiology and Immunology, University of California San Francisco, San Francisco, California, United States of America.;University of Minnesota, United States of America |
| |
| Abstract: | BackgroundActivation-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 FindingsWe 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/SignificanceThese 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. |
| |
| Keywords: | |
|
|
