UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
نویسندگان
چکیده
منابع مشابه
UvrD 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 کاملDNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteins.
The domain structures of the Escherichia coli Rep and Helicase II proteins and their ligand-dependent conformational changes have been examined by monitoring the sensitivity of these helicases to proteolysis by trypsin and chymotrypsin. Limited treatment of unliganded Rep protein (73 kDa) with trypsin results in cleavage at a single site in its carboxyl-terminal region, producing a 68-kDa polyp...
متن کاملPcrA Helicase Dismantles RecA Filaments by Reeling in DNA in Uniform Steps
Translocation of helicase-like proteins on nucleic acids underlies key cellular functions. However, it is still unclear how translocation can drive removal of DNA-bound proteins, and basic properties like the elementary step size remain controversial. Using single-molecule fluorescence analysis on a prototypical superfamily 1 helicase, Bacillus stearothermophilus PcrA, we discovered that PcrA p...
متن کاملResolving Holliday junctions with Escherichia coli UvrD helicase.
The Escherichia coli UvrD helicase is known to function in the mismatch repair and nucleotide excision repair pathways and has also been suggested to have roles in recombination and replication restart. The primary intermediate DNA structure in these two processes is the Holliday junction. UvrD has been shown to unwind a variety of substrates including partial duplex DNA, nicked DNA, forked DNA...
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 کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2004
ISSN: 0261-4189,1460-2075
DOI: 10.1038/sj.emboj.7600485