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Related Experiment Videos

Structural phylogenetic analysis of activation-induced deaminase function.

H Travis Ichikawa1, Mark P Sowden, Andrew T Torelli

  • 1Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|June 21, 2006
PubMed
Summary

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Activation-induced deaminase (AID) evolved the nuclear export signal (NES) before class switch recombination (CSR) activity emerged. Xenopus AID, but not pufferfish AID, can mediate CSR in mouse cells, revealing evolutionary insights into immunoglobulin gene diversification.

Area of Science:

  • Immunology
  • Evolutionary Biology
  • Molecular Biology

Background:

  • Activation-induced deaminase (AID) is crucial for immunoglobulin (Ig) gene diversification in mammals, initiating somatic hypermutation (SHM) and class switch recombination (CSR).
  • Distinct regions within AID govern SHM and CSR activities, with a CRM1-dependent nuclear export signal (NES) at the C terminus being essential for CSR.
  • CSR is a more recent evolutionary development, appearing after the divergence of bony fish, which possess only SHM capabilities.

Purpose of the Study:

  • To investigate the evolutionary origins of CSR activity within AID.
  • To determine if the nuclear export signal (NES) motif predates the emergence of CSR.
  • To identify non-catalytic regions of AID that influence its function in mammalian cells.

Main Methods:

Related Experiment Videos

  • Assessing the ability of Xenopus laevis and Takifugu rubripes AID to induce CSR in AID-deficient mouse B cells.
  • Evaluating the catalytic activity of frog and fish AID in bacterial and mammalian systems.
  • Analyzing the nuclear export of Takifugu AID via CRM1 and testing the functional substitution of its NES motif with human AID.
  • Performing domain-swapping experiments by fusing the Takifugu AID catalytic domain to the human noncatalytic domain.

Main Results:

  • Xenopus laevis AID, but not Takifugu rubripes AID, successfully induced CSR in mouse B cells, despite both exhibiting catalytic activity.
  • Takifugu AID, similar to mammalian AID, undergoes CRM1-dependent nuclear export, and its NES motif is functionally interchangeable with the human NES.
  • Fusion of the Takifugu AID catalytic domain to the human noncatalytic domain restored CSR activity in mammalian cells.

Conclusions:

  • The CSR-essential NES motif in AID evolved prior to the acquisition of CSR activity itself.
  • Non-catalytic regions of AID, beyond the NES, play a significant role in its functional regulation and CSR capability.
  • This study provides critical insights into the evolutionary trajectory of immunoglobulin gene diversification mechanisms.