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Review
. 2003 Sep 15;22(18):4579-83.
doi: 10.1093/emboj/cdg441.

Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes

Martin R Singleton  1 , Dale B Wigley
Affiliations
Review

Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes

Martin R Singleton et al. EMBO J. .

Abstract

Enzymes that operate on nucleic acid substrates are faced with the unusual situation where the substrate is much larger than themselves. Despite the potential to promote catalysis by utilizing the significant binding energy available through their interaction with substrate, ATP hydrolysis is frequently a part of the mechanism of these enzymes. The reasons for this have become clearer in recent years, and a surprising range of ways that these enzymes utilize the free energy of hydrolysis of ATP has been revealed. This review describes these different mechanisms in the context of the biochemical reactions that they support.

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Figures

None
Fig. 1. Examples of ATP-mediated reactions on nucleic acid substrates. (A) A helicase (blue) unwinds base-paired strands of DNA or RNA. (B) A motor protein (blue) dissociates another protein (pink) from the nucleic acid substrate. (C) A chromatin remodelling factor (blue) releases DNA from the nucleosome (purple) to allow the access of other factors (green). (D) RecA protein (blue) may be recycled on the same substrate with concomitant hydrolysis of ATP. (E) DnaB helicase (red) is bound to DnaC (blue). After recruitment to the origin-bound DnaA (yellow), ATP is hydrolysed to allow loading of the helicase onto single-stranded DNA. (F) Two SMC (Structural Maintenance of Chromosomes) head domains (blue) dimerize after binding ATP. (G) Origin unwinding is achieved by the origin recognition complex (ORC) complex (blue) hydrolysing ATP. More detailed descriptions of the mechanisms are given in the text.
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