FoxA proteins are pioneer transcription factors, among the first to bind 
chromatin domains in development and enable gene activity. The Fox DNA-binding 
domain structurally resembles linker histone and binds nucleosomes stably. Using 
fluorescence recovery after photobleaching, we found that FoxA1 and FoxA2 move 
much more slowly in nuclei than other transcription factor types, including 
c-Myc, GATA-4, NF-1, and HMGB1. We find that slower nuclear mobility correlates 
with high nonspecific nucleosome binding, and point mutations that disrupt 
nonspecific binding markedly increase nuclear mobility. FoxA's distinct nuclear 
mobility is consistent with its pioneer activity in chromatin.