Programmable RNA Shredding by the Type III-A CRISPR-Cas System of Streptococcus thermophilus
Immunity against viruses and plasmids provided by CRISPR-Cas systems relies on a ribonucleoprotein effector complex that triggers the degradation of invasive nucleic acids (NA). Effector complexes of type I (Cascade) and II (Cas9-dual RNA) target foreign DNA. Intriguingly, the genetic evidence sugge...
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Published in | Molecular cell Vol. 56; no. 4; pp. 506 - 517 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
20.11.2014
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Abstract | Immunity against viruses and plasmids provided by CRISPR-Cas systems relies on a ribonucleoprotein effector complex that triggers the degradation of invasive nucleic acids (NA). Effector complexes of type I (Cascade) and II (Cas9-dual RNA) target foreign DNA. Intriguingly, the genetic evidence suggests that the type III-A Csm complex targets DNA, whereas biochemical data show that the type III-B Cmr complex cleaves RNA. Here we aimed to investigate NA specificity and mechanism of CRISPR interference for the Streptococcus thermophilus Csm (III-A) complex (StCsm). When expressed in Escherichia coli, two complexes of different stoichiometry copurified with 40 and 72 nt crRNA species, respectively. Both complexes targeted RNA and generated multiple cuts at 6 nt intervals. The Csm3 protein, present in multiple copies in both Csm complexes, acts as endoribonuclease. In the heterologous E. coli host, StCsm restricts MS2 RNA phage in a Csm3 nuclease-dependent manner. Thus, our results demonstrate that the type III-A StCsm complex guided by crRNA targets RNA and not DNA.
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•Streptococcus thermophilus type III-A Csm (StCsm) complex targets RNA•Multiple cuts are introduced in the target RNA at 6 nt intervals•Csm3 protein subunits are responsible for endoribonuclease activity of the complex•StCsm complex offers a programmable tool for RNA degradation
RNA-protein complexes in CRISPR-Cas systems provide immunity against viruses and plasmids. Type I (Cascade) and II (Cas9) complexes target foreign DNA. Tamulaitis et al. demonstrate that the Csm complex (type III-A) of Streptococcus thermophilus targets RNA and establishes a mechanism for RNA degradation. |
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AbstractList | Immunity against viruses and plasmids provided by CRISPR-Cas systems relies on a ribonucleoprotein effector complex that triggers the degradation of invasive nucleic acids (NA). Effector complexes of type I (Cascade) and II (Cas9-dual RNA) target foreign DNA. Intriguingly, the genetic evidence suggests that the type III-A Csm complex targets DNA, whereas biochemical data show that the type III-B Cmr complex cleaves RNA. Here we aimed to investigate NA specificity and mechanism of CRISPR interference for the Streptococcus thermophilus Csm (III-A) complex (StCsm). When expressed in Escherichia coli, two complexes of different stoichiometry copurified with 40 and 72 nt crRNA species, respectively. Both complexes targeted RNA and generated multiple cuts at 6 nt intervals. The Csm3 protein, present in multiple copies in both Csm complexes, acts as endoribonuclease. In the heterologous E. coli host, StCsm restricts MS2 RNA phage in a Csm3 nuclease-dependent manner. Thus, our results demonstrate that the type III-A StCsm complex guided by crRNA targets RNA and not DNA.
[Display omitted]
•Streptococcus thermophilus type III-A Csm (StCsm) complex targets RNA•Multiple cuts are introduced in the target RNA at 6 nt intervals•Csm3 protein subunits are responsible for endoribonuclease activity of the complex•StCsm complex offers a programmable tool for RNA degradation
RNA-protein complexes in CRISPR-Cas systems provide immunity against viruses and plasmids. Type I (Cascade) and II (Cas9) complexes target foreign DNA. Tamulaitis et al. demonstrate that the Csm complex (type III-A) of Streptococcus thermophilus targets RNA and establishes a mechanism for RNA degradation. Immunity against viruses and plasmids provided by CRISPR-Cas systems relies on a ribonucleoprotein effector complex that triggers the degradation of invasive nucleic acids (NA). Effector complexes of type I (Cascade) and II (Cas9-dual RNA) target foreign DNA. Intriguingly, the genetic evidence suggests that the type III-A Csm complex targets DNA, whereas biochemical data show that the type III-B Cmr complex cleaves RNA. Here we aimed to investigate NA specificity and mechanism of CRISPR interference for the Streptococcus thermophilus Csm (III-A) complex (StCsm). When expressed in Escherichia coli, two complexes of different stoichiometry copurified with 40 and 72 nt crRNA species, respectively. Both complexes targeted RNA and generated multiple cuts at 6 nt intervals. The Csm3 protein, present in multiple copies in both Csm complexes, acts as endoribonuclease. In the heterologous E. coli host, StCsm restricts MS2 RNA phage in a Csm3 nuclease-dependent manner. Thus, our results demonstrate that the type III-A StCsm complex guided by crRNA targets RNA and not DNA. |
Author | Nwokeoji, Alison O. Horvath, Philippe Tamulaitis, Gintautas Kazlauskiene, Migle Siksnys, Virginijus Manakova, Elena Venclovas, Česlovas Dickman, Mark J. |
Author_xml | – sequence: 1 givenname: Gintautas surname: Tamulaitis fullname: Tamulaitis, Gintautas organization: Department of Protein–DNA Interactions, Institute of Biotechnology, Vilnius University, Graiciuno 8, Vilnius 02241, Lithuania – sequence: 2 givenname: Migle surname: Kazlauskiene fullname: Kazlauskiene, Migle organization: Department of Protein–DNA Interactions, Institute of Biotechnology, Vilnius University, Graiciuno 8, Vilnius 02241, Lithuania – sequence: 3 givenname: Elena surname: Manakova fullname: Manakova, Elena organization: Department of Protein–DNA Interactions, Institute of Biotechnology, Vilnius University, Graiciuno 8, Vilnius 02241, Lithuania – sequence: 4 givenname: Česlovas surname: Venclovas fullname: Venclovas, Česlovas organization: Department of Bioinformatics, Institute of Biotechnology, Vilnius University, Graiciuno 8, Vilnius 02241, Lithuania – sequence: 5 givenname: Alison O. surname: Nwokeoji fullname: Nwokeoji, Alison O. organization: Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Mappin Street, Sheffield S1 3JD, UK – sequence: 6 givenname: Mark J. surname: Dickman fullname: Dickman, Mark J. organization: Department of Chemical and Biological Engineering, ChELSI Institute, University of Sheffield, Mappin Street, Sheffield S1 3JD, UK – sequence: 7 givenname: Philippe surname: Horvath fullname: Horvath, Philippe organization: DuPont Nutrition and Health, BP10, Dangé-Saint-Romain 86220, France – sequence: 8 givenname: Virginijus surname: Siksnys fullname: Siksnys, Virginijus email: siksnys@ibt.lt organization: Department of Protein–DNA Interactions, Institute of Biotechnology, Vilnius University, Graiciuno 8, Vilnius 02241, Lithuania |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25458845$$D View this record in MEDLINE/PubMed |
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Snippet | Immunity against viruses and plasmids provided by CRISPR-Cas systems relies on a ribonucleoprotein effector complex that triggers the degradation of invasive... |
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SubjectTerms | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Clustered Regularly Interspaced Short Palindromic Repeats CRISPR-Associated Proteins - chemistry CRISPR-Associated Proteins - genetics CRISPR-Associated Proteins - metabolism Endoribonucleases - genetics Endoribonucleases - metabolism Molecular Sequence Data Protein Binding Protein Structure, Quaternary RNA Cleavage Scattering, Small Angle Streptococcus thermophilus - enzymology Streptococcus thermophilus - genetics X-Ray Diffraction |
Title | Programmable RNA Shredding by the Type III-A CRISPR-Cas System of Streptococcus thermophilus |
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