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Studying Biologically Templated Materials with Atomic Force Microscopy
Published in Sivashankar Krishnamoorthy, Krzysztof Iniewski, Nanomaterials, 2017
Andrew J. Lee, Christoph Walti
A promising approach is to utilize the Escherichia coli protein Recombinase A (RecA) for spatially addressing DNA architectures.54 The RecA protein is involved in DNA repair pathways through homologous recombination. It polymerizes upon single-stranded DNA in the presence of ATP and magnesium to form a nucleoprotein filament. Subsequently, this nucleoprotein complex is able to self-assemble onto a double-stranded DNA at regions of shared homology between the encapsulated single-stranded DNA and the double-stranded DNA (Figure 3.5a). Upon successful assembly, the two homologous strands exchange resulting in the substitution of the new single-stranded DNA molecule with the homologous region of the double-stranded DNA molecule, and then the RecA complex disassociates through the hydrolysis of ATP.
Multiple inhibitory effects of succinic acid on Microcystis aeruginosa: morphology, metabolomics, and gene expression
Published in Environmental Technology, 2022
Yi-dong Chen, Chu Zhao, Xiao-yu Zhu, Yuan Zhu, Ru-nan Tian
The recA gene encodes a highly conserved and multifunctional RecA protein, which plays a key role in DNA repair and initiates the SOS response to DNA damage [41]. Studies have shown that the expression of recA will be up-regulated when the environmental stress is not serious but down-regulated under severe environmental stress [42, 43]. In this study, the recA transcription decreased significantly after treatment with 60 mg L−1 SA for 3 h, and then returned to the control level at 24 h. It is possible that the Microcystis cells sensed the SA stress in a short period of time, which caused the expression to decrease. With extended exposure time, the cells became adapted to this stress, and the expression returned to the control level.