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FEBS Lett. 2012 Nov 16;586(22):3956-61. doi: 10.1016/j.febslet.2012.09.041. Epub 2012 Oct 16.

Nucleic acid binding surface and dimer interface revealed by CRISPR-associated CasB protein structures.

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1
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14850, USA.

Abstract

The CRISPR system is an adaptive RNA-based microbial immune system against invasive genetic elements. CasB is an essential protein component in Type I-E Cascade. Here, we characterize CasB proteins from three different organisms as non-specific nucleic acid binding proteins. The Thermobifida fusca CasB crystal structure reveals conserved positive surface charges, which we show are important for its nucleic acid binding function. EM docking reveals that CasB dimerization aligns individual nucleic acid binding surfaces into a curved, elongated binding surface inside Type I-E Cascade, consistent with the putative functions of CasB in ds-DNA recruitment and crRNA-DNA duplex formation steps.

PMID:
23079036
PMCID:
PMC3878058
DOI:
10.1016/j.febslet.2012.09.041
[Indexed for MEDLINE]
Free PMC Article
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