Structural characterization of the type I-B CRISPR Cas7 from Thermobaculum terrenum

Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements. A heterologous ribonucleoprotein silencing complex composed of CRISPR-associated (Cas) proteins and a CRISPR RNA (crRNA) neutralizes the inco...

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Published inBiochimica et biophysica acta. Proteins and proteomics Vol. 1871; no. 3; p. 140900
Main Authors Seo, Pil-Won, Gu, Do-Heon, Kim, Ji-Won, Kim, Jun-Hong, Park, Suk-Youl, Kim, Jeong-Sun
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.05.2023
Subjects
Bacteria
Binding Sites
Cas7
Cascade
CRISPR
Csh2
RNA
CRISPR
Csh2
Cas7
Cascade
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Abstract Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements. A heterologous ribonucleoprotein silencing complex composed of CRISPR-associated (Cas) proteins and a CRISPR RNA (crRNA) neutralizes the incoming mobile genetic elements. The type I and III silencing complexes commonly include a protein-helical backbone of several copies of identical subunits, for example, Cas7 in the type I silencing complex. In this study, we structurally characterized type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2). The revealed crystal structure of TterCsh2 shows a typical glove-like architecture of Cas7, which consists of a palm, a thumb, and a finger domain. Csh2 proteins have 5 conserved sequence motifs that are arranged to form a presumable crRNA-binding site in the TterCsh2 structure. This crRNA binding site of TterCsh2 is structurally and potentially comparable to those observed in helix-forming Cas7 structures in other sub-types. Analysis of the reported Cas7 structures and their sequences suggests that Cas7s can be divided into at least two sub-classes. These data will broaden our understanding on the Cascade complex of CRISPR/Cas systems. •Crystal structure of Cascade backbone-forming type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2) was determined.•TterCsh2 adopts a typical folding of Cas7.•TterCsh2 is structurally and sequentially more similar to type I-C Cas7 than to those of type I-E and I-F.•Comparative analysis of TterCsh2 with reported Cas7s suggests that Cas7 can be divided into at least two sub-classes.
AbstractList Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements. A heterologous ribonucleoprotein silencing complex composed of CRISPR-associated (Cas) proteins and a CRISPR RNA (crRNA) neutralizes the incoming mobile genetic elements. The type I and III silencing complexes commonly include a protein-helical backbone of several copies of identical subunits, for example, Cas7 in the type I silencing complex. In this study, we structurally characterized type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2). The revealed crystal structure of TterCsh2 shows a typical glove-like architecture of Cas7, which consists of a palm, a thumb, and a finger domain. Csh2 proteins have 5 conserved sequence motifs that are arranged to form a presumable crRNA-binding site in the TterCsh2 structure. This crRNA binding site of TterCsh2 is structurally and potentially comparable to those observed in helix-forming Cas7 structures in other sub-types. Analysis of the reported Cas7 structures and their sequences suggests that Cas7s can be divided into at least two sub-classes. These data will broaden our understanding on the Cascade complex of CRISPR/Cas systems. •Crystal structure of Cascade backbone-forming type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2) was determined.•TterCsh2 adopts a typical folding of Cas7.•TterCsh2 is structurally and sequentially more similar to type I-C Cas7 than to those of type I-E and I-F.•Comparative analysis of TterCsh2 with reported Cas7s suggests that Cas7 can be divided into at least two sub-classes.
Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements. A heterologous ribonucleoprotein silencing complex composed of CRISPR-associated (Cas) proteins and a CRISPR RNA (crRNA) neutralizes the incoming mobile genetic elements. The type I and III silencing complexes commonly include a protein-helical backbone of several copies of identical subunits, for example, Cas7 in the type I silencing complex. In this study, we structurally characterized type I-B Cas7 (Csh2 from Thermobaculum terrenum; TterCsh2). The revealed crystal structure of TterCsh2 shows a typical glove-like architecture of Cas7, which consists of a palm, a thumb, and a finger domain. Csh2 proteins have 5 conserved sequence motifs that are arranged to form a presumable crRNA-binding site in the TterCsh2 structure. This crRNA binding site of TterCsh2 is structurally and potentially comparable to those observed in helix-forming Cas7 structures in other sub-types. Analysis of the reported Cas7 structures and their sequences suggests that Cas7s can be divided into at least two sub-classes. These data will broaden our understanding on the Cascade complex of CRISPR/Cas systems.
ArticleNumber 140900
Author Seo, Pil-Won
Gu, Do-Heon
Kim, Ji-Won
Kim, Jeong-Sun
Kim, Jun-Hong
Park, Suk-Youl
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Keywords CRISPR
Csh2
Cas7
Cascade
Language English
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Snippet Clustered regularly interspaced short palindromic repeats (CRISPR) in many prokaryotes functions as an adaptive immune system against mobile genetic elements....
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StartPage 140900
SubjectTerms Bacteria
Binding Sites
Cas7
Cascade
CRISPR
Csh2
RNA
Title Structural characterization of the type I-B CRISPR Cas7 from Thermobaculum terrenum
URI https://dx.doi.org/10.1016/j.bbapap.2023.140900
https://www.ncbi.nlm.nih.gov/pubmed/36682394
https://search.proquest.com/docview/2768817828
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