XPD helicase speeds through a molecular traffic jam

Mol Cell. 2009 Sep 11;35(5):549-50. doi: 10.1016/j.molcel.2009.08.012.

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.

Publication types

  • Comment

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / metabolism*
  • Binding Sites
  • DNA / chemistry
  • DNA / metabolism*
  • DNA Repair*
  • Kinetics
  • Models, Molecular
  • Nucleic Acid Conformation
  • Replication Protein A / chemistry
  • Replication Protein A / metabolism*
  • Spectrometry, Fluorescence
  • Xeroderma Pigmentosum Group D Protein / chemistry
  • Xeroderma Pigmentosum Group D Protein / metabolism*

Substances

  • Archaeal Proteins
  • Replication Protein A
  • Adenosine Triphosphate
  • DNA
  • Xeroderma Pigmentosum Group D Protein