In silico analysis ofPlasmodiumspecies specific UvrD helicase
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چکیده
منابع مشابه
In silico analysis of Plasmodium species specific UvrD helicase
Malaria is still a devastating disease caused by the mosquito-transmitted parasite Plasmodium, particularly Plasmodium falciparum. During the last few years the situation has worsened in many ways, mainly due to malarial parasites becoming increasingly resistant to several anti-malarial drugs. Thus there is an urgent need to find alternate ways to control malaria and therefore it is necessary t...
متن کاملUvrD helicase
In classical bacterial nucleotide excision repair (NER), a bulky DNA lesion such as a UV photoproduct is recognized by the UvrAB DNA damage recognition complex, and the strand containing the adduct is incised by UvrC nuclease upstream and downstream of the lesion. UvrD helicase subsequently loads at a nicked DNA site and unwinds the 12-base pair duplex containing the lesion, thereby creating a ...
متن کاملUvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli.
The roles of UvrD and Rep DNA helicases of Escherichia coli are not yet fully understood. In particular, the reason for rep uvrD double mutant lethality remains obscure. We reported earlier that mutations in recF, recO or recR genes suppress the lethality of uvrD rep, and proposed that an essential activity common to UvrD and Rep is either to participate in the removal of toxic recombination in...
متن کاملCharacterization of a thermostable UvrD helicase and its participation in helicase-dependent amplification.
Helicase-dependent amplification (HDA) is an isothermal in vitro DNA amplification method based upon the coordinated actions of helicases to separate double-stranded DNA and DNA polymerases to synthesize DNA. Previously, a mesophilic form of HDA (mHDA) utilizing the Escherichia coli UvrD helicase, DNA polymerase I Klenow fragment, two accessory proteins, MutL and single-stranded DNA-binding pro...
متن کاملLarge domain movements upon UvrD dimerization and helicase activation.
Escherichia coli UvrD DNA helicase functions in several DNA repair processes. As a monomer, UvrD can translocate rapidly and processively along ssDNA; however, the monomer is a poor helicase. To unwind duplex DNA in vitro, UvrD needs to be activated either by self-assembly to form a dimer or by interaction with an accessory protein. However, the mechanism of activation is not understood. UvrD c...
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ژورنال
عنوان ژورنال: Communicative & Integrative Biology
سال: 2013
ISSN: 1942-0889
DOI: 10.4161/cib.23125