PMID:21472697: Difference between revisions

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<span style = 'font-size: large'> '''Lohman, GJ, Tabor, S and Nichols, NM'''  (2011) DNA ligases.''Curr Protoc Mol Biol'' '''Chapter 3''':Unit3.14</span>
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|{{TableHeadingColor}} |'''Abstract''' || <protect>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.</protect>
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'''Lohman, GJ, Tabor, S and Nichols, NM''' (2011) DNA ligases. ''Curr Protoc Mol Biol'' '''Chapter 3''':Unit3.14
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!align=left  |Abstract
*  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21472697 PubMed]
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21472697 PubMed]
Online version:[http://dx.doi.org/10.1002/0471142727.mb0314s94 10.1002/0471142727.mb0314s94]
Online version:[http://dx.doi.org/10.1002/0471142727.mb0314s94 10.1002/0471142727.mb0314s94]
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!align=left  |Keywords
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Bacteriophages/enzymology; Bacteriophages/genetics; DNA Ligases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/metabolism; Genetic Techniques/instrumentation; Viral Proteins/metabolism
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Latest revision as of 04:38, 15 September 2013

Citation

Lohman, GJ, Tabor, S and Nichols, NM (2011) DNA ligases. Curr Protoc Mol Biol Chapter 3:Unit3.14

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.

Links

PubMed Online version:10.1002/0471142727.mb0314s94

Keywords

Bacteriophages/enzymology; Bacteriophages/genetics; DNA Ligases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/metabolism; Genetic Techniques/instrumentation; Viral Proteins/metabolism

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