The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity

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The DnaE polymerase from Deinococcus radiodurans features RecA-dependent DNA polymerase activity

We report in the present study on the catalytic properties of the Deinococcus radiodurans DNA polymerase III α subunit (αDr). The αDr enzyme was overexpressed in Escherichia coli, both in soluble form and as inclusion bodies. When purified from soluble protein extracts, αDr was found to be tightly associated with E. coli RNA polymerase, from which αDr could not be dissociated. On the contrary, ...

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DNA helicase activity of the RecD protein from Deinococcus radiodurans.

The bacterium Deinococcus radiodurans is extremely resistant to high levels of DNA-damaging agents, including gamma rays and ultraviolet light that can lead to double-stranded DNA breaks. Surprisingly, the organism does not appear to have a RecBCD enzyme, an enzyme that is critical for double-strand break repair in many other bacteria. The D. radiodurans genome does encode a protein whose close...

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The RecA proteins of Deinococcus radiodurans and Escherichia coli promote DNA strand exchange via inverse pathways.

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ژورنال

عنوان ژورنال: Bioscience Reports

سال: 2016

ISSN: 0144-8463,1573-4935

DOI: 10.1042/bsr20160364