Proteins participate in extensive networks of protein-protein interactions in the cell. Transient protein interactions are defined by their temporal interaction with other proteins and are more difficult to identify using physical methods like pull-down assay, an invaluable tool to study protein-protein interactions. Fortunately, chemical cross-linking provides the means for capturing these transient interactions. A combination of chemical crosslinking and pull-down assay allows us to demonstrate interactions between the SWI/SNF chromatin remodeling complex (1) and DNA damage recognition factors in Saccharomyces cerevisiae. Chromatin forms a repressive structure that tends to limit the access of DNA-binding proteins to DNA in eukaryotic nuclei (2). Our findings suggest that chromatin remodeling activities are recruited to overcome the inhibitory effect of nucleosomes on DNA repair. Chromatin remodeling factors are likely to be involved in chromatin rearrangement during NER (3,4).