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[26] [28] The most known SF1A helicases are Rep and UvrD in gram-negative bacteria and PcrA helicase from gram-positive bacteria. [26] The most known Helicases in the SF1B group are RecD and Dda helicases. [26] They have a RecA-like-fold core. [27] Superfamily 2 (SF2): This is the largest group of helicases that are involved in varied cellular ...
DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication.Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. [1]
In ICP8, the herpes simplex virus (HSV-1) single-strand DNA-binding protein (ssDNA-binding protein (SSB)), the head consists of the eight alpha helices.The front side of the neck region consists of a five-stranded beta-sheet and two alpha helices, whereas the back side is a three-stranded beta-sheet The shoulder part of the N-terminal domain contains an alpha-helical and beta-sheet region. [1]
RecBCD is unusual amongst helicases because it has two helicases that travel with different rates [6] and because it can recognize and be altered by the Chi DNA sequence. [7] [8] RecBCD avidly binds an end of linear double-stranded (ds) DNA. The RecD helicase travels on the strand with a 5' end at which the enzyme initiates unwinding, and RecB ...
A) Circular bacterial chromosomes contain a cis-acting element, the replicator, that is located at or near replication origins. i) The replicator recruits initiator proteins in a DNA sequence-specific manner, which results in melting of the DNA helix and loading of the replicative helicase onto each of the single DNA strands (ii).
RecQ helicase is a family of helicase enzymes initially found in Escherichia coli [1] that has been shown to be important in genome maintenance. [ 2 ] [ 3 ] [ 4 ] They function through catalyzing the reaction ATP + H 2 O → ADP + P and thus driving the unwinding of paired DNA and translocating in the 3' to 5' direction.
DEAD box proteins were first brought to attention in the late 1980s in a study that looked at a group of NTP binding sites that were similar in sequence to the eIF4A RNA helicase sequence. [4] The results of this study showed that these proteins (p68, SrmB, MSS116, vasa, PL10, mammalian eIF4A, yeast eIF4A) involved in RNA metabolism had several ...
In bacteria, the main component of the pre-RC is DnaA. The pre-RC is complete when DnaA occupies all of its binding sites within the bacterial origin of replication . The particular sites on the oriC that DnaA binds to determines if the cell has a bORC (bacterial Origin Recognition Complex) or a pre-RC. [1]