1 H, 13 C, 15 N backbone and side chain resonance assignment of the HNH nuclease from Streptococcus pyogenes CRISPR-Cas9

Biomolecular NMR Assignments
Helen B BelatoGeorge P Lisi

Abstract

HNH is one of two endonuclease domains of the clustered regularly interspaced short palindromic repeats (CRISPR)-associated protein Cas9 that perform site-specific cleavage of double-stranded DNA. We engineered a novel construct of this critical nuclease from Streptococcus pyogenes Cas9 that not only maintains the wild-type amino acid sequence and fold, but displays enhanced thermostability when compared to the full-length Cas9 enzyme. Here, we report backbone and side chain assignments of the HNH nuclease as a foundational step toward the characterization of protein dynamics and allostery in CRISPR-Cas9.

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Citations

Jan 31, 2021·Nature Communications·Santrupti NerliNikolaos G Sgourakis
Dec 31, 2019·Journal of the American Chemical Society·Kyle W EastGeorge P Lisi

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