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

Nam KH, Huang Q, Ke A
FEBS Lett 586 3956-61 (2012)
Cited: 16 times
EuropePMC logo PMID: 23079036

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.

Reviews - 4h79 mentioned but not cited (1)

  1. Structure Principles of CRISPR-Cas Surveillance and Effector Complexes. Tsui TK, Li H. Annu Rev Biophys 44 229-255 (2015)

Articles - 4h79 mentioned but not cited (3)



Reviews citing this publication (5)

  1. Adaptation in CRISPR-Cas Systems. Sternberg SH, Richter H, Charpentier E, Qimron U. Mol Cell 61 797-808 (2016)
  2. CRISPR interference: a structural perspective. Reeks J, Naismith JH, White MF. Biochem J 453 155-166 (2013)
  3. DNA and RNA interference mechanisms by CRISPR-Cas surveillance complexes. Plagens A, Richter H, Charpentier E, Randau L. FEMS Microbiol Rev 39 442-463 (2015)
  4. Exploiting CRISPR/Cas: interference mechanisms and applications. Richter H, Randau L, Plagens A. Int J Mol Sci 14 14518-14531 (2013)
  5. Exploiting DNA Endonucleases to Advance Mechanisms of DNA Repair. Thompson MK, Sobol RW, Prakash A. Biology (Basel) 10 530 (2021)

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