Marked dependence on growth state of backup pathways of NHEJ

Int J Radiat Oncol Biol Phys. 2007 Aug 1;68(5):1462-70. doi: 10.1016/j.ijrobp.2007.04.038.

Abstract

Purpose: Backup pathways of nonhomologous end joining (B-NHEJ) enable cells to repair DNA double-strand breaks (DSBs) when DNA-PK-dependent NHEJ (D-NHEJ) is compromised. Recent evidence implicates growth signaling in the regulation of D-NHEJ. This study was intended to determine whether the ability to repair DSBs by B-NHEJ also depends on growth state.

Methods and materials: LIG4(-/-) and wild type (WT) mouse embryo fibroblasts (MEFs) were used. Repair of DSBs was measured by pulsed-field agarose gel electrophoresis. G1 cells were selected by centrifugal elutriation. A plasmid assay was used to measure DNA end-joining activity in whole cell extracts.

Results: Wild-type MEFs efficiently repaired DSBs by D-NHEJ in either the exponential or plateau phase of growth. Because of their defect in ligase IV, which compromises D-NHEJ, LIG4(-/-) MEFs showed reduced repair capacity but were slowly able to rejoin a large proportion of DSBs via B-NHEJ. B-NHEJ was markedly reduced in the plateau phase of growth or at high radiation doses. Elutriated G1 cells from exponentially growing or plateau-phase LIG4(-/-) cultures showed a response similar to nonelutriated cells, ruling out that the effect simply reflects redistribution in the cell cycle. An in vitro assay, gauging the activity of B-NHEJ, showed a reduction in DNA end joining during the plateau phase that could be corrected by recombinant DNA ligase IIIalpha.

Conclusions: Suppression of growth signaling markedly compromises DSB repair by B-NHEJ. This effect is associated with a reduction in DNA ligase III mediated DNA end joining.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • DNA Ligase ATP
  • DNA Ligases / deficiency
  • DNA Ligases / physiology*
  • DNA Repair / physiology*
  • DNA-Binding Proteins / physiology*
  • Electrophoresis, Gel, Pulsed-Field / methods
  • Embryo, Mammalian
  • Fibroblasts / cytology
  • Fibroblasts / enzymology
  • Fibroblasts / physiology*
  • G1 Phase
  • Mice
  • Poly-ADP-Ribose Binding Proteins
  • Xenopus Proteins

Substances

  • DNA-Binding Proteins
  • Poly-ADP-Ribose Binding Proteins
  • XLF protein, mouse
  • Xenopus Proteins
  • DNA Ligases
  • DNA Ligase ATP
  • DNA ligase III alpha protein, Xenopus
  • Lig3 protein, mouse