Biochim Biophys Acta. 1988 Dec 20;951(2-3):330-4.

Multiple roles of DNA ligase at the replication fork.

Montecucco A, Pedrali-Noy G, Spadari S, Ciarrocchi G.

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Istituto di Genetica Biochimica ed Evoluzionistica, CNR, Pavia, Italy.

Abstract

The loss of superhelical turns from a covalently closed duplex DNA exposed to bacteriophage T4 DNA ligase in the presence of AMP and Mg2+ has recently been found to be gradual and not sudden (Montecucco, A. and Ciarrocchi, G. (1988) Nucleic Acids Res. 16, 7369-7381). In this paper, we show that the AMP-dependent DNA relaxation catalyzed by human and E. coli DNA ligases also takes place according to a step-wise mechanism. DNA relaxation is inhibited by pyrophosphate, by ATP (or NAD in the case of the E. coli enzyme) and by high ionic strength and is essentially distributive with the human or T4 DNA ligases, and processive with the bacterial one. The AMP-dependent ability of DNA ligases to relax DNA might allow these enzymes to relieve possible topological complications of the nascent double helix generated by the replication of the lagging strand.

PMID:: 3145019; [PubMed - indexed for MEDLINE]

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AMP-dependent DNA relaxation catalyzed by DNA ligase occurs by a nicking-closing mechanism. [Nucleic Acids Res. 1988]
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Montecucco A, Ciarrocchi G. Nucleic Acids Res. 1988 Aug 11; 16(15):7369-81.
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Review DNA ligase: structure, mechanism, and function.
Lehman IR. Science. 1974 Nov 29; 186(4166):790-7.
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Review DNA-joining enzymes: a review.
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Multiple roles of DNA ligase at the replication fork.

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