<i>Aci</i>l, a unique restriction endonuclease from<i>Arthrobacter citreus</i>which recognizes 5′ CCGC 3′

Polisson, Carol; Morgan, Richard D.

doi:10.1093/nar/18.19.5911

Cited by 5 publications

(3 citation statements)

References 2 publications

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“…We chose the endonuclease AciI, which can only recognize double-stranded structures, to cleave S•S* (cleavage site: S strand, 5′-C ̂CGC-3′; S* strand, 5′-G ̂CGG-3′). 48 We first verified that AciI can cleave S•S* in solution by ingel fluorescence experiments using L1 and L2 C-Cy5 : the band of the cross-linked hybrids at high molecular weight disappeared (lane 5, Figure 2F). We then investigated the effect of AciI treatment on FRET signals using the L S pair.…”

Section: Depatching Of Lipid Raftsmentioning

confidence: 79%

“…In contrast to the antibody-based , or peptide self-assembly-based lipid raft patching strategies, , our method enables the cleavage of the DNA linkages between CTxB nodes using restriction endonucleases, thereby realizing lipid raft depatching in living cells (Figure E). We chose the endonuclease AciI, which can only recognize double-stranded structures, to cleave S·S* (cleavage site: S strand, 5′-ĈCGC-3′; S* strand, 5′-ĜCGG-3′) . We first verified that AciI can cleave S·S* in solution by in-gel fluorescence experiments using L1 and L2 C‑Cy5 : the band of the cross-linked hybrids at high molecular weight disappeared (lane 5, Figure F).…”

Section: Resultsmentioning

confidence: 98%

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A Patching and Coding Lipid Raft-Localized Universal Imaging Platform

Zhong,

Chen,

Yan

et al. 2023

Chemical & Biomedical Imaging

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Lipid rafts (LRs) are relatively well-ordered functional microdomains in cell membranes and play an irreplaceable role in physiological processes as a transduction platform for multiple signaling pathways. Due to their small size and high spatiotemporal dynamics, it is difficult to perform lipid raftlocalized biomolecule imaging on the surface of living cells. Here, we report a DNA nanotechnology-based platform for reversible manipulation and localized analysis of lipid rafts, which consists of two modules: "patching and coding probe pair" and "fishing probe". The probe pair is generated by modifying two different sets of connectable DNA structures on a lipid raft-specific protein.After recognizing lipid rafts, the two probes in close proximity are linked by a DNA ligase reaction to form a lipid raft identity (LR-ID) code. The LR-ID strand patches and stabilizes the lipid raft structure. Interestingly, the raft patches formed can be depatched by restriction endonucleases, providing the first reversible manipulation of the lipid raft structure in living cells. We also designed a "fishing probe" with a DNA hairpin structure using an aptamer that can specifically bind to the target. The probe can cascade the reaction to two input signals "LR-ID" and "target protein" to generate an "off−on" fluorescence switch, allowing imaging and dynamic monitoring of target proteins localized in lipid rafts. By encoding arbitrary targets (in the case of glycans) in lipid rafts, we have created a universal lipid raft-localized imaging platform. This work provides an integrated analytical and manipulative platform to reveal lipid rafts and associated signaling pathways at the molecular level.

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Section: Depatching Of Lipid Raftsmentioning

confidence: 79%

Section: Resultsmentioning

confidence: 98%

A Patching and Coding Lipid Raft-Localized Universal Imaging Platform

Zhong,

Chen,

Yan

et al. 2023

Chemical & Biomedical Imaging

View full text Add to dashboard Cite

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“…The purified PCR products were also used for digestion with the restriction endonucleases Acil and Nael (New England Biolabs, Beverly, MA, USA), which cleave the nucleotide sequence 5'..C/C-G-C/C-G-G/C..3' at the first C-C (Acil) and (Nael) second C-G (Polisson and Morgan, 1990;New England Biolabs, 1993. Approximately 1 ,ug of product was digested with 5-10 units of the enzymes for 3 h at 37°C and was subjected to electrophoresis on 12% acrylamide gels (Sambrook et al, 1989).…”

Section: Methodsmentioning

confidence: 99%

Hot-spot mutations in the p53 gene of liver nodules induced in rats fed DL-ethionine with a methyl-deficient diet

Tsujiuchi

Yeleswarapu²,

Y³

et al. 1997

Br J Cancer

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Summary Male F-344 rats were fed for 15 weeks a methyl-deficient L-amino acid defined diet containing 0.05% DL-ethionine. Nodules protruding from the surface of the liver were dissected free of surrounding tissue, and polyadenylated RNA isolated from the nodules was reverse transcribed. The region of the p53 gene comprising codons 120-290 was amplified by the polymerase chain reaction, and cDNAs were sequenced. Mutations were detected in nodules obtained from 7 of 12 rats. In all seven cases, the same two point mutations were present. The first was at the first base of codon 246 and consisted of a C-*T transition (C:G--T:A, Arg-*Cys), while the second was at the second base of codon 247 and consisted of a G-*T transversion (G:C->T:A, Arg->Leu). It is concluded that the hepatocarcinogen ethionine induces specific hot-spot p53 gene mutations; this is in contrast to the mutations at various sites previously observed to occur in rats fed a hepatocarcinogenic methyl-deficient diet alone. The results also provide the first evidence that ethionine is mutagenic in the rat.

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Restriction enzymes and their isoschizomers

Roberts¹

1990

Nucleic Acids Research

197

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Acil, a unique restriction endonuclease fromArthrobacter citreuswhich recognizes 5′ CCGC 3′

Cited by 5 publications

References 2 publications

A Patching and Coding Lipid Raft-Localized Universal Imaging Platform

A Patching and Coding Lipid Raft-Localized Universal Imaging Platform

Hot-spot mutations in the p53 gene of liver nodules induced in rats fed DL-ethionine with a methyl-deficient diet

Restriction enzymes and their isoschizomers

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