Abstract
Hexameric helicases control both the initiation and the elongation phase of DNA replication. The toroidal structure of these enzymes provides an inherent challenge in the opening and loading onto DNA at origins, as well as the conformational changes required to exclude one strand from the central channel and activate DNA unwinding. Recently, high-resolution structures have not only revealed the architecture of various hexameric helicases but also detailed the interactions of DNA within the central channel, as well as conformational changes that occur during loading. This structural information coupled with advanced biochemical reconstitutions and biophysical methods have transformed our understanding of the dynamics of both the helicase structure and the DNA interactions required for efficient unwinding at the replisome.
Subject
General Pharmacology, Toxicology and Pharmaceutics,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine
Reference128 articles.
1. Did DNA replication evolve twice independently?;D Leipe;Nucleic Acids Res.,1999
2. Viral proteins containing the purine NTP-binding sequence pattern.;A Gorbalenya;Nucleic Acids Res.,1989
3. The bacterial replicative helicase DnaB evolved from a RecA duplication.;D Leipe;Genome Res.,2000
4. Evolutionary relationships and structural mechanisms of AAA+ proteins.;J Erzberger;Annu Rev Biophys Biomol Struct.,2006
5. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.;A Neuwald;Genome Res.,1999
Cited by
22 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献