title: XPD helicase speeds through a molecular traffic jam.
abstract: Helicases and other DNA translocases must travel along crowded substrates. In this issue, Honda et al. (2009) report that the archaeal XPD helicase can bypass a single-stranded DNA-binding protein without either molecule being ejected from the DNA.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
authors.forename: Ilya J
authors.initials: IJ
authors.lastname: Finkelstein
authors.forename: Eric C
authors.initials: EC
authors.lastname: Greene
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004260:DNA Repair; D007700:Kinetics; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D051716:Replication Protein A / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D051759:Xeroderma Pigmentosum Group D Protein / Q000737:chemistry / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D051716:Replication Protein A; D000255:Adenosine Triphosphate; D004247:DNA; D051759:Xeroderma Pigmentosum Group D Protein