title: Mapping physical interactions within chromatin by proteomic approaches.
abstract: Our ability to study protein-protein interactions has grown by leaps and bounds in recent years, enabling numerous large-scale studies to be performed in a variety of organisms. Despite this success, some classes of proteins, including those bound to chromatin, remain difficult to characterize through proteomic approaches. Some of the problems faced by researchers studying chromatin-bound proteins include low complex solubility, heterogeneous sample composition, and numerous transient interactions, which can be further complicated by the presence of DNA itself. To tackle these issues, a number of innovative protocols have been developed to better study the various facets of chromatin biology. In this review, we will discuss novel approaches to study protein-DNA interactions as well as protein complexes affecting chromatin.
authors.affiliation: Samuel Lunenfeld Research Institute at Mount Sinai Hospital, Toronto, ON, Canada.
authors.forename: Jean-Philippe
authors.initials: JP
authors.lastname: Lambert
authors.forename: Tony
authors.initials: T
authors.lastname: Pawson
authors.forename: Anne-Claude
authors.initials: AC
authors.lastname: Gingras
mesh_terms: D000818:Animals; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D025941:Protein Interaction Mapping / Q000379:methods*; D040901:Proteomics / Q000379:methods*
chemical_list: D002843:Chromatin; D006657:Histones