Journal
MOLECULAR MICROBIOLOGY
Volume 84, Issue 1, Pages 6-16Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2958.2012.08012.x
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Funding
- Wellcome Trust [091968/Z/10/Z]
- BBSRC [BB/E006450/1] Funding Source: UKRI
- Wellcome Trust [091968/Z/10/Z] Funding Source: Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/E006450/1] Funding Source: researchfish
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Threading of DNA through the central channel of a replicative ring helicase is known as helicase loading, and is a pivotal event during replication initiation at replication origins. Once loaded, the helicase recruits the primase through a direct proteinprotein interaction to complete the initial priming step of DNA replication. Subsequent assembly of the polymerases and processivity factors completes the structure of the replisome. Two replisomes are assembled, one on each strand, and move in opposite directions to replicate the parental DNA during the elongation step of DNA replication. Replicative helicases are the motor engines of replisomes powered by the conversion of chemical energy to mechanical energy through ATP binding and hydrolysis. Bidirectional loading of two ring helicases at a replication origin is achieved by strictly regulated and intricately choreographed mechanisms, often through the action of replication initiation and helicase-loader proteins. Current structural and biochemical data reveal a wide range of different helicase-loading mechanisms. Here we review advances in this area and discuss their implications.
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