Abstract
Helicases are molecular motor proteins that couple NTP hydrolysis to directional movement along nucleic acids. A class of helicases characterized by their ring-shaped hexameric structures translocate processively and unidirectionally along single-stranded (ss) DNA to separate the strands of double-stranded (ds) DNA, aiding both in the initiation and fork progression during DNA replication. These replicative ring-shaped helicases are found from virus to human. We review recent biochemical and structural studies that have expanded our understanding on how hexameric helicases use the NTPase reaction to translocate on ssDNA, unwind dsDNA, and how their physical and functional interactions with the DNA polymerase and primase enzymes coordinate replication of the two strands of dsDNA.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Publication types
-
Research Support, N.I.H., Extramural
-
Review
MeSH terms
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism*
-
Bacteriophage T7 / chemistry
-
Bacteriophage T7 / genetics
-
Bacteriophage T7 / metabolism*
-
DNA / genetics
-
DNA / metabolism
-
DNA Helicases / chemistry
-
DNA Helicases / genetics
-
DNA Helicases / metabolism*
-
DNA Primase / chemistry
-
DNA Primase / genetics
-
DNA Primase / metabolism*
-
DNA Replication / genetics*
-
DNA, Single-Stranded / genetics
-
DNA, Single-Stranded / metabolism
-
DNA-Directed DNA Polymerase / chemistry
-
DNA-Directed DNA Polymerase / genetics
-
DNA-Directed DNA Polymerase / metabolism*
-
Humans
-
Kinetics
-
Models, Molecular
-
Molecular Motor Proteins / chemistry
-
Molecular Motor Proteins / genetics
-
Molecular Motor Proteins / metabolism*
-
Protein Conformation
-
Viral Proteins / chemistry
-
Viral Proteins / genetics
-
Viral Proteins / metabolism*
Substances
-
Bacterial Proteins
-
DNA, Single-Stranded
-
Molecular Motor Proteins
-
Okazaki fragments
-
Viral Proteins
-
DNA
-
DNA Primase
-
DNA-Directed DNA Polymerase
-
DNA Helicases