Browse

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

Cited 5 time in Web of Science Cited 5 time in Scopus
Authors
Min, Kyungjin; Yoon, Hyunjun; Jo, Inseong; Ha, Nam-Chul; Jin, Kyeong Sik; Kim, Jin-Soo; Lee, Hyung Ho
Issue Date
2018-04
Citation
Biochemical and Biophysical Research Communications, Vol.498 No.4, pp.775-781
Keywords
Cpf1CRISPR-Cas systemGenome-editingSAXSElectron microscopy
Abstract
Clustered regularly interspaced short palindromic repeats (CRISPRs) from Prevotella and Francisella (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. (C) 2018 Elsevier Inc. All rights reserved.
ISSN
0006-291X
URI
https://hdl.handle.net/10371/165705
DOI
https://doi.org/10.1016/j.bbrc.2018.03.057
Files in This Item:
There are no files associated with this item.
Appears in Collections:
Seoul National University(서울대학교)Featured Researcher's Articles
  • mendeley

Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse