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• W2131504992 startingPage "2635" @default.
• W2131504992 abstract "The RecQ helicase from Deinococcus radiodurans (DrRecQ) distinguishes from other helicases in that it utilizes its three 'helicase and RNaseD C-terminal' domains (HRDC1, HRDC2 and HRDC3) to regulate its activity. These HRDC domains have different influence on the biochemical functions of DrRecQ. Currently, only the structure of HRDC3 was reported. Here, we determined the NMR structure of the N-terminal-most HRDC1, revealing a potential DNA binding domain. Fluorescence anisotropy assay indicates that HRDC1 has binding affinity weaker than 70 μM to all DNA substrates without any specificity. Biochemical assays suggested that HRDC1 cooperates with other domains to enhance full-length DrRecQ interactions with DNA." @default.
• W2131504992 created "2016-06-24" @default.
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• W2131504992 date "2013-07-04" @default.
• W2131504992 modified "2023-09-23" @default.
• W2131504992 title "NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans" @default.
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• W2131504992 doi "https://doi.org/10.1016/j.febslet.2013.06.048" @default.
• W2131504992 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23831579" @default.
• W2131504992 hasPublicationYear "2013" @default.
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