Asset Details
Do you wish to reserve the book?
Minichromosome Maintenance Helicase Activity Is Controlled by N-and C-Terminal Motifs and Requires the ATPase Domain Helix-2 Insert
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?
Minichromosome Maintenance Helicase Activity Is Controlled by N-and C-Terminal Motifs and Requires the ATPase Domain Helix-2 Insert
Do you wish to request the book?
Minichromosome Maintenance Helicase Activity Is Controlled by N-and C-Terminal Motifs and Requires the ATPase Domain Helix-2 Insert
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
Minichromosome Maintenance Helicase Activity Is Controlled by N-and C-Terminal Motifs and Requires the ATPase Domain Helix-2 Insert
2006
Overview
The minichromosome maintenance (MCM) proteins are essential conserved proteins required for DNA replication in archaea and eukaryotes. MCM proteins are believed to provide the replicative helicase activity that unwinds template DNA ahead of the replication fork. Consistent with this hypothesis, MCM proteins can form hexameric complexes that possess ATP-dependent DNA unwinding activity. The molecular mechanism by which the energy of ATP hydrolysis is harnessed to DNA unwinding is unknown, although the ATPase activity has been attributed to a highly conserved AAA+ family ATPase domain. Here we show that changes to Nand C-terminal motifs in the single MCM protein from the archaeon Methanothermobacter thermautotrophicus (MthMCM) can modulate ATP hydrolysis, DNA binding, and duplex unwinding. Furthermore, these motifs appear to influence the movement of the β-α-β insert in helix-2 of the MCM ATPase domain. Removal of this motif from MthMCM increased dsDNA-stimulated ATP hydrolysis and increased the affinity of the mutant complex for ssDNA and dsDNA. Deletion of the helix-2 insert additionally resulted in the abrogation of DNA unwinding. Our results provide significant insight into the molecular mechanisms used by the MCM helicase to both regulate and execute DNA unwinding.
Publisher
National Academy of Sciences
Subject
/ Adenosine Triphosphatases - metabolism
/ Archaea
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ ATP
/ Cell Cycle Proteins - chemistry
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ DNA
/ Methanobacteriaceae - enzymology
/ Proteins
We currently cannot retrieve any items related to this title. Kindly check back at a later time.