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A Population of Thermostable Reverse Transcriptases Evolved from Thermus aquaticus DNA Polymerase I by Phage Display

Authors

  • Sophie Vichier-Guerre Dr.,

    1. Unité de Chimie Organique URA 2128 CNRS, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris 15, France, Fax: (+33) 145-688-404
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  • Stéphane Ferris,

    1. Unité de Chimie Organique URA 2128 CNRS, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris 15, France, Fax: (+33) 145-688-404
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  • Nicolas Auberger,

    1. Unité de Chimie Organique URA 2128 CNRS, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris 15, France, Fax: (+33) 145-688-404
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  • Karim Mahiddine,

    1. Unité de Chimie Organique URA 2128 CNRS, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris 15, France, Fax: (+33) 145-688-404
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  • Jean-Luc Jestin Dr.

    1. Unité de Chimie Organique URA 2128 CNRS, Département de Biologie Structurale et Chimie, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris 15, France, Fax: (+33) 145-688-404
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Errata

This article is corrected by:

  1. Errata: A Population of Thermostable Reverse Transcriptases Evolved from Thermus aquaticus DNA Polymerase I by Phage Display Volume 49, Issue 7, 1184, Article first published online: 1 February 2010

  • We thank F. Bahrami, M. Delarue, P. A. Kaminski, and S. Wain-Hobson for critical comments on the manuscript, T. Huynh-Dinh and P. E. Bost for advice, and C. Gouyette, O. Helynck, and V. Huteau for technical help. This work was supported by the Ministère de la Recherche (ACI blanche), the CNRS (Programme Physique et Chimie du Vivant), and the Pasteur–Weizmann Foundation.

Abstract

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Running in reverse: A set of enzymes selected according to their RNA-dependent DNA polymerase activity from a library of more than 107 mutant enzymes has been characterized. The product was specifically bound to catalytically active proteins displayed on filamentous bacteriophage. The selected variants have a catalytic efficiency for reverse transcription that is two orders of magnitude higher.

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