Impediment of Replication Forks by Long Non-coding RNA Provokes Chromosomal Rearrangements by Error-Prone Restart

Cell Rep. 2017 Nov 21;21(8):2223-2235. doi: 10.1016/j.celrep.2017.10.103.

Abstract

Naturally stalled replication forks are considered to cause structurally abnormal chromosomes in tumor cells. However, underlying mechanisms remain speculative, as capturing naturally stalled forks has been a challenge. Here, we captured naturally stalled forks in tumor cells and delineated molecular processes underlying the structural evolution of circular mini-chromosomes (double-minute chromosomes; DMs). Replication forks stalled on the DM by the co-directional collision with the transcription machinery for long non-coding RNA. RPA, BRCA2, and DNA polymerase eta (Polη) were recruited to the stalled forks. The recruitment of Polη was critical for replication to continue, as Polη knockdown resulted in DM loss. Rescued stalled forks were error-prone and switched replication templates repeatedly to create complex fusions of multiple short genomic segments. In mice, such complex fusions circularized the genomic region surrounding MYC to create a DM during tumorigenesis. Our results define a molecular path that guides stalled replication forks to complex chromosomal rearrangements.

Keywords: DNA damage tolerance; double-minute chromosomes; gross chromosomal rearrangements; replication-transcription conflicts; stalled replication forks.

MeSH terms

  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / metabolism
  • Acid Anhydride Hydrolases
  • Animals
  • BRCA2 Protein / metabolism*
  • Chromosome Aberrations*
  • DNA Repair / genetics*
  • DNA Replication / genetics*
  • DNA-Binding Proteins / metabolism
  • Mice
  • RNA, Long Noncoding / genetics
  • RNA, Long Noncoding / metabolism*
  • Rad51 Recombinase / genetics
  • Rad51 Recombinase / metabolism

Substances

  • ATP-Binding Cassette Transporters
  • BRCA2 Protein
  • BRCA2 protein, human
  • DNA-Binding Proteins
  • RNA, Long Noncoding
  • Rad51 Recombinase
  • Rad51 protein, mouse
  • Acid Anhydride Hydrolases
  • Rad50 protein, mouse