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Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle.

The periodic destruction of RAG-2 at the G1-to-S transition couples V(D)J recombination to the G0 and G1 cell cycle phases and coordinates RAG-mediated DNA cleavage with DNA repair by nonhomologous end joining. To define the mechanism by which this occurs, we reproduced cell cycle-dependent regulation of the V(D)J recombinase in a cell-free system. The ubiquitin-proteasomal pathway carries out destruction of RAG-2 in lysates of S phase cells and during S phase in vivo. Remarkably, the Skp2-SCF ubiquitin ligase, which plays a central role in cell cycle regulation through the destruction of p27, mediates ubiquitylation of RAG-2 in vitro and degradation of RAG-2 in vivo. The regulation of antigen receptor gene assembly by Skp2-SCF provides an unexpected and direct mechanistic link between DNA recombination and the cell cycle.

Pubmed ID: 15949444


  • Jiang H
  • Chang FC
  • Ross AE
  • Lee J
  • Nakayama K
  • Nakayama K
  • Desiderio S


Molecular cell

Publication Data

June 10, 2005

Associated Grants


Mesh Terms

  • Cell Cycle
  • DNA-Binding Proteins
  • G1 Phase
  • HeLa Cells
  • Humans
  • Nuclear Proteins
  • Recombination, Genetic
  • S Phase
  • S-Phase Kinase-Associated Proteins
  • Ubiquitin
  • VDJ Recombinases