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Structural insights into the apo-structure of Cpf1 protein from Francisella novicida

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Title
Structural insights into the apo-structure of Cpf1 protein from Francisella novicida
Author(s)
Min, K; Yoon, H; Jo, I; Ha, NC; Jin, KS; Kim, JS; Lee, HH
Publication Date
2018-04
Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.498, no.4, pp.775 - 781
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Abstract
Clustered regularly interspaced short palindromic repeats (CRISPRs) from Prevotella and Francisella 1 (Cpf1) are RNA-guided endonucleases that produce cohesive double-stranded breaks in DNA by specifically recognizing thymidine-rich protospacer-adjacent motif (PAM) sequences. Cpf1 is emerging as a powerful genome-editing tool. Despite previous structural studies on various Cpf1 proteins, the apo-structure of Cpf1 remains unknown. In the present study, we determined the solution structure of the Cpf1 protein from Francisella novicida (FnCpf1) with and without CRISPR RNA (crRNA) using small-angle X-ray scattering, providing the insights into the apo-structure of FnCpf1. The apo-structure of FnCpf1 was also visualized using negative staining electron microcopy. When we compared the apo-structure of FnCpf1 with crRNA-bound structure, their overall shapes (a closed form) were similar, suggesting that conformational change upon crRNA binding to FnCpf1 is not drastic, but a local induced fit might occur to recognize PAM sequences. In contrast, the apo Cpf1 from Moraxella bovoculi 237 (MbCpf1) was analyzed as an open form, implying that a large conformational change from an open to a closed form might be required for crRNA binding to MbCpf1. These results suggested that the crRNA-induced conformational changes in Cpf1 differ among species. © 2018 Elsevier Inc
URI
https://pr.ibs.re.kr/handle/8788114/5457
ISSN
0006-291X
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Center for Genome Engineering(유전체 교정 연구단) > Journal Papers (저널논문)
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