ArticleStructure (London, England : 1993)2019
Mechanism of Filamentation-Induced Allosteric Activation of the SgrAI Endonuclease.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Activation of the SPARDA defense system by filament assembly using a beta-relay signaling mechanism widespread in prokaryotic Argonautes.Cell research · 2025Article
- Structure, identification and characterization of the RibD-enolase complex inbioRxiv : the preprint server for biology · 2025Article
- Two-metal ion mechanism of DNA cleavage by activated, filamentous SgrAI.The Journal of biological chemistry · 2024Article
- Light-sensitive phosphorylation regulates retinal IMPDH1 activity and filament assembly.The Journal of cell biology · 2024Article
- Discovery, structure, and function of filamentous 3-methylcrotonyl-CoA carboxylase.Structure (London, England : 1993) · 2023Article
- The role of filamentation in activation and DNA sequence specificity of the sequence-specific endonuclease SgrAI.Biochemical Society transactions · 2022Article
- The structure of the human LACTB filament reveals the mechanisms of assembly and membrane binding.PLoS biology · 2022Article
- Pretransition state and apo structures of the filament-forming enzyme SgrAI elucidate mechanisms of activation and substrate specificity.The Journal of biological chemistry · 2022Article
- Novel insights into filament-forming enzymes.Nature reviews. Molecular cell biology · 2020Review
- Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation.Biophysical reviews · 2019Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Filament formation by enzymes is increasingly recognized as an important phenomenon with potentially unique regulatory properties and biological roles. SgrAI is an allosterically regulated type II restriction endonuclease that forms filaments with enhanced DNA cleavage activity and altered sequence specificity. Here, we present the cryoelectron microscopy (cryo-EM) structure of the filament of SgrAI in its activated configuration. The structural data illuminate the mechanistic origin of hyperaccelerated DNA cleavage activity and suggests how indirect DNA sequence readout within filamentous SgrAI may enable recognition of substantially more nucleotide sequences than its low-activity form, thereby altering and partially relaxing its DNA sequence specificity. Together, substrate DNA binding, indirect readout, and filamentation simultaneously enhance SgrAI's catalytic activity and modulate substrate preference. This unusual enzyme mechanism may have evolved to perform the specialized functions of bacterial innate immunity in rapid defense against invading phage DNA without causing damage to the host DNA.
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Registered trials
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