Asset Details
Do you wish to reserve the book?
Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid
Do you wish to request the book?
Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid
2010
Overview
The mechanism leading to protein-primed DNA replication has been studied extensively in vitro. However, little is known about the in vivo organization of the proteins involved in this fundamental process. Here we show that the terminal proteins (TPs) of phages φ29 and PRD1, infecting the distantly related bacteria Bacillus subtilis and Escherichia coli, respectively, associate with the host bacterial nucleoid independently of other viral-encoded proteins. Analyses of phage φ29 revealed that the TP N-terminal domain (residues 1—73) possesses sequence-independent DNA-binding capacity and is responsible for its nucleoid association. Importantly, we show that in the absence of the TP N-terminal domain the efficiency of φ29 DNA replication is severely affected. Moreover, the TP recruits the phage DNA polymerase to the bacterial nucleoid, and both proteins later are redistributed to enlarged helix-like structures in an MreB cytoskeleton-dependent way. These data disclose a key function for the TP in vivo: organizing the early viral DNA replication machinery at the cell nucleoid.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Bacillus Phages - physiology
/ Bacillus subtilis - genetics
/ Bacillus subtilis - metabolism
/ Bacillus subtilis - virology
/ Bacteriophage PRD1 - genetics
/ Bacteriophage PRD1 - physiology
/ DNA
/ DNA Replication - physiology
/ DNA-Directed DNA Polymerase - metabolism
/ E coli
/ Escherichia coli - metabolism
/ Genomes
/ Mutation
/ Phages
/ Proteins
/ Recombinant Fusion Proteins - genetics
/ Recombinant Fusion Proteins - metabolism
/ Virus Replication - genetics
/ Virus Replication - physiology
/ Viruses
We currently cannot retrieve any items related to this title. Kindly check back at a later time.