ArticleMolecular cell2022
PAM binding ensures orientational integration during Cas4-Cas1-Cas2-mediated CRISPR adaptation.
Article in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Single nucleotide variants drive evolutionary phage-host arms race in anaerobic carbon dioxide-converting microbiome.Nature communications · 2026Article
- Insights into spacer acquisition of the type V-A CRISPR-Cas system of Francisella novicida U112.Nucleic acids research · 2026Article
- Structures reveal how the Cas1-2/3 integrase captures, delivers, and integrates foreign DNA into CRISPR loci.Structure (London, England : 1993) · 2025Article
- Discovery of CRISPR-Cas12a clades using a large language model.Nature communications · 2025Article
- Functional insights into Solo-Cas4 inmicroLife · 2025Article
- Article
- Harnessing CRISPR-Cas adaptation for RNA recording and beyond.BMB reports · 2024Review
- Structure reveals why genome folding is necessary for site-specific integration of foreign DNA into CRISPR arrays.Nature structural & molecular biology · 2023Article
- Cas4/1 dual nuclease activities enable prespacer maturation and directional integration in a type I-G CRISPR-Cas system.bioRxiv : the preprint server for biology · 2023Article
- Genome expansion by a CRISPR trimmer-integrase.Nature · 2023Article
- Structural snapshots of R-loop formation by a type I-C CRISPR Cascade.Molecular cell · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Adaptation in CRISPR-Cas systems immunizes bacteria and archaea against mobile genetic elements. In many DNA-targeting systems, the Cas4-Cas1-Cas2 complex is required for selection and processing of DNA segments containing PAM sequences prior to integration of these "prespacer" substrates as spacers in the CRISPR array. We determined cryo-EM structures of the Cas4-Cas1-Cas2 adaptation complex from the type I-C system that encodes standalone Cas1 and Cas4 proteins. The structures reveal how Cas4 specifically reads out bases within the PAM sequence and how interactions with both Cas1 and Cas2 activate Cas4 endonuclease activity. The Cas4-PAM interaction ensures tight binding between the adaptation complex and the prespacer, significantly enhancing integration of the non-PAM end into the CRISPR array and ensuring correct spacer orientation. Corroborated with our biochemical results, Cas4-Cas1-Cas2 structures with substrates representing various stages of CRISPR adaptation reveal a temporally resolved mechanism for maturation and integration of functional spacers into the CRISPR array.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.