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A Programmable Dual-RNA–Guided DNA Endonuclease in Adaptive Bacterial Immunity
TLDR
This study reveals a family of endonucleases that use dual-RNAs for site-specific DNA cleavage and highlights the potential to exploit the system for RNA-programmable genome editing.
DNA interrogation by the CRISPR RNA-guided endonuclease Cas9
TLDR
It is shown that both binding and cleavage of DNA by Cas9–RNA require recognition of a short trinucleotide protospacer adjacent motif (PAM) and that PAM interactions trigger Cas9 catalytic activity.
Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease
TLDR
A crystal structure of Streptococcus pyogenes Cas9 in complex with a single-molecule guide RNA and a target DNA containing a canonical 5′-NGG-3′ PAM is reported, revealing that the PAM motif resides in a base-paired DNA duplex.
Structures of Cas9 Endonucleases Reveal RNA-Mediated Conformational Activation
TLDR
To compare the architectures and domain organization of diverse Cas9 proteins, the atomic structures of Cas9 from Streptococcus pyogenes and Actinomyces naeslundii and AnaCas9 were determined by x-ray crystallography and three-dimensional reconstructions of apo-SpyCas9, SpyCas9:RNA, and SpyCas 9:RNA:DNA were obtained by negative-stain single-particle electron microscopy.
RNA-programmed genome editing in human cells
TLDR
It is shown here that Cas9 assembles with hybrid guide RNAs in human cells and can induce the formation of double-strand DNA breaks at a site complementary to the guide RNA sequence in genomic DNA.
Sequence- and Structure-Specific RNA Processing by a CRISPR Endonuclease
TLDR
The RNA recognition mechanism identified here explains sequence- and structure-specific processing by a large family of CRISPR-specific endoribonucleases.
A three-dimensional view of the molecular machinery of RNA interference
TLDR
The molecular structures of Dicer and the Argonaute proteins, free and bound to small RNAs, have offered exciting insights into the molecular mechanisms that are central to RNA silencing pathways.
Structural biology of nucleocytoplasmic transport.
TLDR
The molecular mechanisms underlying nucleocytoplasmic transport as they have been revealed by structural studies of the receptors and regulators in different steps of transport cycles are described.
The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin α
TLDR
The crystal structure of the homodimeric TPR domain of human OGT, which contains 11.5 TPR repeats, is solved and it is proposed that OGT uses an analogous molecular mechanism to recognize its targets.
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