Influence of the C‑Terminal Tail of RecA Proteins from Alkaline pH-Resistant Bacterium Deinococcus Ficus
| Autor: | Shu Su, Hsiu-Fang Fan, Cyuan-Ji Chen, Ying-An Kuo |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
biology
DNA damage General Chemical Engineering Ficus Deinococcus radiodurans General Chemistry biochemical phenomena metabolism and nutrition biology.organism_classification medicine.disease_cause chemistry.chemical_compound Chemistry chemistry Biochemistry medicine bacteria Deinococcus ficus Deinococcus Escherichia coli QD1-999 DNA Bacteria |
| Zdroj: | ACS Omega, Vol 5, Iss 31, Pp 19868-19876 (2020) |
| ISSN: | 2470-1343 |
| Popis: | Deinococcus ficus CC-FR2-10T, resistant to ultraviolet, ionizing radiation, and chemicals which may cause DNA damage, was identified in Taiwan. The expression level of D. ficus RecA, which has 92% sequence identity with Deinococcus radiodurans (Dr.) RecA, will be upregulated upon UV radiation. Multiple sequence alignment of RecA proteins from bacteria belonging to Escherichia coli and the Deinococcus genus reveals that the C-terminal tail of D. ficus RecA is shorter and contains less acidic residues than E. coli RecA. D. ficus RecA exhibits a higher ATPase activity toward single-stranded (ss) DNA and efficiently promotes DNA strand exchange that a filament is first formed on ssDNA, followed by uptake of the double-stranded (ds) substrate. Moreover, D. ficus RecA exhibits a pH-reaction profile for DNA strand exchange similar to E. coli ΔC17 RecA. Later, a chimera D. ficus C17 E. coli RecA with more acidic residues in the C-terminal tail was constructed and purified. Increased negativity in the C-terminal tail makes the pH reaction profile for Chimera D. ficus C17 E. coli RecA DNA strand exchange exhibit a reaction optimum similar to E. coli RecA. To sum up, D. ficus RecA exhibits reaction properties in substrate-dependent ATPase activity and DNA strand exchange similar to E. coli RecA. Our data indicate that the negativity in the C-terminal tail plays an important role in the regulation of pH-dependent DNA strand exchange activity. |
| Databáze: | OpenAIRE |
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