C. elegans provides an excellent model system for the study of the Fanconi 
Anemia (FA), one of the hallmarks of which is sensitivity to interstrand 
crosslinking agents. Central to our understanding of FA has been the 
investigation of DOG-1, the functional ortholog of the deadbox helicase FANCJ. 
Here we review the current understanding of the unique role of DOG-1 in 
maintaining stability of G-rich DNA in C. elegans and explore the question of 
why DOG-1 animals are crosslink sensitive. We propose a dynamic model in which 
noncovalently linked G-rich structures form and un-form in the presence of 
DOG-1. When DOG-1 is absent but crosslinking agents are present the G-rich 
structures are readily covalently crosslinked, resulting in increased crosslinks 
formation and thus giving increased crosslink sensitivity. In this 
interpretation DOG-1 is neither upstream nor downstream in the FA pathway, but 
works alongside it to limit the availability of crosslink substrates. This model 
reconciles the crosslink sensitivity observed in the absence of DOG-1 function 
with its unique role in maintaining G-Rich DNA and will help to formulate 
experiments to test this hypothesis.