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两种形式的激活诱导胞嘧啶脱氨酶,其结合琼脂糖的能力不同。

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

机构信息

Nikolaus-Fiebiger Center, Department of Internal Medicine III, Division of Molecular Immunology, University of Erlangen-Nürnberg, Erlangen, Germany.

出版信息

PLoS One. 2010 Jan 27;5(1):e8883. doi: 10.1371/journal.pone.0008883.

Abstract

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.

摘要

背景

激活诱导胞嘧啶脱氨酶(AID)是一种 B 细胞特异性 DNA 突变酶,在生发中心 B 细胞中次级抗体库的形成中发挥关键作用。在寻找结合伴侣时,通常使用琼脂糖珠进行蛋白共免疫沉淀检测。

方法/主要发现:我们发现,无论检测的细胞裂解液中是否含有外源性或内源性 AID,两种小鼠 AID 形式之一均可单独与琼脂糖结合。

结论/意义:这些结合特性可能归因于 AID 的已知翻译后修饰;在共免疫沉淀实验中也需要考虑这些特性,以避免假阳性结果。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3068/2811734/02757f057105/pone.0008883.g001.jpg

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