The structural biology of CRISPR-Cas systems.
Prokaryotic CRISPR-Cas genomic loci encode RNA-mediated adaptive immune systems that bear some functional similarities with eukaryotic RNA interference. Acquired and heritable immunity against bacteriophage and plasmids begins with integration of ∼30 base pair foreign DNA sequences into the host genome. CRISPR-derived transcripts assemble with CRISPR-associated (Cas) proteins to target complementary nucleic acids for degradation. Here we review recent advances in the structural biology of these targeting complexes, with a focus on structural studies of the multisubunit Type I CRISPR RNA-guided surveillance and the Cas9 DNA endonuclease found in Type II CRISPR-Cas systems. These complexes have distinct structures that are each capable of site-specific double-stranded DNA binding and local helix unwinding.
Department of Molecular & Cell Biology, University of California, Berkeley, CA 94720, USA.
Fuguo
F
Jiang
Department of Molecular & Cell Biology, University of California, Berkeley, CA 94720, USA; Department of Chemistry, University of California, Berkeley, CA 94720, USA; Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute (HHMI), University of California, Berkeley, CA 94720, USA. Electronic address: doudna@berkeley.edu.
Jennifer A
JA
Doudna
D064130:CRISPR-Associated Proteins / Q000737:chemistry*; D064113:CRISPR-Cas Systems / Q000235:genetics* / Q000502:physiology*; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D018390:Gene Targeting / Q000379:methods*; D008958:Models, Molecular
D064130:CRISPR-Associated Proteins