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Regulation of anti-CRISPR operons by structurally distinct families of Aca proteins

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dc.contributor.authorSo Yeon Lee-
dc.contributor.authorNils Birkholz-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorPeter C. Fineran-
dc.contributor.authorHyun Ho Park-
dc.date.accessioned2026-02-10T04:21:03Z-
dc.date.available2026-02-10T04:21:03Z-
dc.date.issued2025-11-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/16603-
dc.description.abstractCRISPR-Cas systems provide bacteria with adaptive immunity against bacteriophages and mobile genetic elements, driving an evolutionary arms race in which phages deploy anti-CRISPR (Acr) proteins. Acr proteins are often co-encoded in operons with anti-CRISPR-associated (Aca) proteins, which coordinate the regulation of acr gene expression. Here, we reveal the molecular basis of DNA binding that mediates transcriptional repression by two distinct Aca family members: Aca7 and Aca11. Crystal structures of Aca7 and Aca11 highlight conserved helix-turn-helix (HTH) motifs within α-helix bundles, providing a universal DNA-binding platform. Aca7 forms a symmetrical dimer to recognize a 19-bp inverted repeat (IR) within the acrIF11-aca7 operon. Strikingly, Aca11 binds 22-bp IRs in two distinct promoters, suggesting that Aca proteins can control multiple target operons. Mutagenesis and electrophoretic mobility shift assays (EMSAs) confirm that dimerization and sequence-specific IR recognition are essential for DNA binding. Despite mechanistic similarities, these and other Aca proteins exhibit notable differences. Structural comparisons across Aca families reveal that while monomer structures are generally similar with conserved HTH motifs, the structures of their dimeric functional units vary significantly. These structural differences might be essential for Aca proteins to bind to various promoters and regulate the expression of different Acr proteins.en_US
dc.languageEnglishen_US
dc.subject.classification해당사항없음en_US
dc.titleRegulation of anti-CRISPR operons by structurally distinct families of Aca proteinsen_US
dc.title.alternativeAca 단백질이 CRISPR 유전자 발현을 조절하는 구조적·분자적 원리 규명en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationSo Yeon Lee, et al. 2025. "Regulation of anti-CRISPR operons by structurally distinct families of Aca proteins". <em>Communications Biology</em>, 8(1698): 0-0.-
dc.citation.titleCommunications Biologyen_US
dc.citation.volume8en_US
dc.citation.number1698en_US
dc.identifier.doihttps://doi.org/10.1038/s42003-025-09101-9-
dc.citation.startPage0en_US
dc.citation.endPage0en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2023:0en_US
dc.subject.keywordAcr proteinen_US
dc.subject.keywordCRISPR-Cas systemen_US
dc.subject.keywordCrystal structureen_US
dc.subject.keywordDNA-bindingen_US
dc.subject.keywordhelix-turn-helix motifen_US
dc.identifier.localId2025-0198-
Appears in Collections  
2025-2025, 극지/해양 생명자원 유래 저온성 미생물/효소를 이용한 환경유해물질 검출 및 정화방법 연구 (25-25) / 이준혁 (PE25150)
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