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


RESULTS
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
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.
Metzner
Mirjam
M
Nikolaus-Fiebiger Center, Department of Internal Medicine III, Division of Molecular Immunology, University of Erlangen-Nürnberg, Erlangen, Germany. mirjam.metzner@ucsf.edu
Schuh
Wolfgang
W
Roth
Edith
E
Jäck
Hans-Martin
HM
Wabl
Matthias
M
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D003564:Cytidine Deaminase / Q000378:metabolism*; D047468:Immunoprecipitation; D007527:Isoenzymes / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012685:Sepharose / Q000378:metabolism*; D000098830:AICDA (Activation-Induced Cytidine Deaminase)
D007527:Isoenzymes; D012685:Sepharose; D000098830:AICDA (Activation-Induced Cytidine Deaminase); D003564:Cytidine Deaminase