Two forms of activation-induced cytidine deaminase differing in their ability to bind agarose

两种活化诱导的胞苷脱氨酶,其结合琼脂糖的能力不同

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作者:Mirjam Metzner, Wolfgang Schuh, Edith Roth, Hans-Martin Jäck, Matthias Wabl

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

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.

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