| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1256574 | Current Opinion in Chemical Biology | 2011 | 6 Pages |
The archaeal DNA replication apparatus is a simplified version of that of eukaryotes and has attracted attention as a tractable model system for the orthologous, but significantly more complex eukaryal machinery. A variety of archaeal model organisms have been investigated with strong emphasis on structural and biochemical analyses of replication-associated proteins. In this review we will describe recent advances in understanding the properties of the replicative helicase, the MCM complex, and the role of the sliding clamp, PCNA, in mediating a range of protein–DNA transactions. Although both complexes form ring shaped assemblies, they play very distinct roles at the leading and trailing edges of the replication fork machinery respectively.
► Archaeal MCM is a homohexameric helicase. ► A series of switches transduce information between DNA binding and ATPase sites. ► PCNA coordinates a range of client proteins. ► A macromolecular assembly of PCNA and three clients may mediate Okazaki fragment maturation.
