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Science 1 November 1996:
Vol. 274. no. 5288, pp. 777 - 780
DOI: 10.1126/science.274.5288.777

Reports

Change of a Catalytic Reaction Carried Out by a DNA Replication Protein

Marie-Françoise Noirot-Gros * and Stanislav D. Ehrlich dagger

The RepA protein of plasmid pC194 initiates and terminates rolling circle replication. At initiation, it forms a 5'-phosphotyrosyl DNA link, whereas at termination, a glutamate residue directs hydrolytic cleavage of the newly synthesized origin, and the resulting 3'-hydroxyl group undergoes transesterification with the phosphotyrosine link. The protein is thus released from DNA, and the termination is uncoupled from reinitiation of replication. Replacement of the glutamate with tyrosine in RepA altered this mechanism, so that termination occurred by two successive transesterifications and became coupled to reinitiation. This result suggests that various enzymes involved in DNA cleavage and rejoining may have similar mechanistic and evolutionary roots.

Génétique Microbienne, Institut National de la Recherche Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France.
*   Present address: Department of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.

dagger    To whom correspondence should be addressed.


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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members.
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Role of Individual Monomers of a Dimeric Initiator Protein in the Initiation and Termination of Plasmid Rolling Circle Replication.
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Replication and Control of Circular Bacterial Plasmids.
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Rolling-circle transposons in eukaryotes.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)