Unit

UNIT 3.14 DNA Ligases

  1. Gregory J.S. Lohman1,
  2. Stanley Tabor2,
  3. Nicole M. Nichols1

Published Online: 1 APR 2011

DOI: 10.1002/0471142727.mb0314s94

Current Protocols in Molecular Biology

Current Protocols in Molecular Biology

How to Cite

Lohman, G. J., Tabor, S. and Nichols, N. M. 2011. DNA Ligases. Current Protocols in Molecular Biology. 94:III:3.14:3.14.1–3.14.7.

Author Information

  1. 1

    New England Biolabs, Ipswich, Massachusetts

  2. 2

    Harvard Medical School, Boston, Massachusetts

Publication History

  1. Published Online: 1 APR 2011
  2. Published Print: APR 2011

Abstract

The DNA ligase enzyme family catalyzes the formation of a phosphodiester bond between juxtaposed 5′-phosphate and 3′-hydroxyl termini in duplex DNA. This activity can seal nicks in duplex DNA or join double-stranded DNA fragments having either blunt or cohesive ends. DNA ligases are central enzymes in molecular biology, nucleic acid research, and in next-generation sequencing applications. Reaction conditions and applications for T4 DNA ligase, E. coli DNA ligase, and thermostable DNA ligases are described in this unit. These enzymes differ in their cofactor requirements, substrate specificity, and thermal stability. Curr. Protoc. Mol. Biol. 94:3.14.1-3.14.7. © 2011 by John Wiley & Sons, Inc.

Keywords:

  • T4 DNA ligase;
  • Taq DNA ligase;
  • DNA ligation;
  • blunt-end ligation;
  • cloning