Recent insight into the kinetic mechanisms and conformational dynamics of Y-Family DNA polymerases
BA Maxwell, Z Suo - Biochemistry, 2014 - ACS Publications
The kinetic mechanisms by which DNA polymerases catalyze DNA replication and repair
have long been areas of active research. Recently discovered Y-family DNA polymerases …
have long been areas of active research. Recently discovered Y-family DNA polymerases …
Dynamic conformational change regulates the protein-DNA recognition: an investigation on binding of a Y-family polymerase to its target DNA
Protein-DNA recognition is a central biological process that governs the life of cells. A
protein will often undergo a conformational transition to form the functional complex with its …
protein will often undergo a conformational transition to form the functional complex with its …
Multidomain protein solves the folding problem by multifunnel combined landscape: Theoretical investigation of a Y-family DNA polymerase
Approximately three-fourths of eukaryotic proteins are composed of multiple independently
folded domains. However, much of our understanding is based on single domain proteins or …
folded domains. However, much of our understanding is based on single domain proteins or …
Investigating the conformational dynamics of a Y-family DNA polymerase during its folding and binding to DNA and a nucleotide
During DNA polymerization, the Y-family DNA polymerases are capable of bypassing
various DNA damage, which can stall the replication fork progression. It has been well …
various DNA damage, which can stall the replication fork progression. It has been well …
Confinement and crowding effects on folding of a multidomain Y-family DNA polymerase
Proteins in vivo endure highly various interactions from the luxuriant surrounding
macromolecular cosolutes. Confinement and macromolecular crowding are the two major …
macromolecular cosolutes. Confinement and macromolecular crowding are the two major …
DNA binding strength increases the processivity and activity of a Y-Family DNA polymerase
J Wu, A De Paz, BM Zamft, AH Marblestone… - Scientific reports, 2017 - nature.com
DNA polymerase (pol) processivity, ie, the bases a polymerase extends before falling off the
DNA, and activity are important for copying difficult DNA sequences, including simple …
DNA, and activity are important for copying difficult DNA sequences, including simple …
Stability and conformational resilience of protein disulfide isomerase
J Guyette, B Evangelista, SA Tatulian, K Teter - Biochemistry, 2019 - ACS Publications
Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and
chaperone activities. It is a U-shaped protein with an abb′ xa′ structural organization in …
chaperone activities. It is a U-shaped protein with an abb′ xa′ structural organization in …
Investigating the trade-off between folding and function in a multidomain Y-family DNA polymerase
The way in which multidomain proteins fold has been a puzzling question for decades. Until
now, the mechanisms and functions of domain interactions involved in multidomain protein …
now, the mechanisms and functions of domain interactions involved in multidomain protein …
Dynamics and thermal stability of the bypass polymerase, DinB homolog (Dbh)
J Soto, SL Moro, MJ Cocco - Frontiers in Molecular Biosciences, 2024 - frontiersin.org
The DinB homolog polymerase (Dbh) is a member of the Y-family of translesion DNA
polymerases that can synthesize using a damaged DNA template. Since Dbh comes from …
polymerases that can synthesize using a damaged DNA template. Since Dbh comes from …
Conformational dynamics of a Y-family DNA polymerase during substrate binding and catalysis as revealed by interdomain Forster resonance energy transfer
BA Maxwell, C Xu, Z Suo - Biochemistry, 2014 - ACS Publications
Numerous kinetic, structural, and theoretical studies have established that DNA
polymerases adjust their domain structures to enclose nucleotides in their active sites and …
polymerases adjust their domain structures to enclose nucleotides in their active sites and …