Terminal Deoxynucleotidyl Transferase: The Story of a Misguided DNA Polymerase
Identifieur interne : 001D17 ( Main/Curation ); précédent : 001D16; suivant : 001D18Terminal Deoxynucleotidyl Transferase: The Story of a Misguided DNA Polymerase
Auteurs : Edward A. Motea [États-Unis] ; Anthony J. Berdis [États-Unis]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2009.
Abstract
Nearly every DNA polymerase characterized to date exclusively catalyzes the incorporation of mononucleotides into a growing primer using a DNA or RNA template as a guide to direct each incorporation event. There is, however, one unique DNA polymerase designated terminal deoxynucleotidyl transferase that performs DNA synthesis using
Url:
DOI: 10.1016/j.bbapap.2009.06.030
PubMed: 19596089
PubMed Central: 2846215
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PMC:2846215Le document en format XML
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<author><name sortKey="Motea, Edward A" sort="Motea, Edward A" uniqKey="Motea E" first="Edward A." last="Motea">Edward A. Motea</name>
<affiliation wicri:level="2"><nlm:aff id="A1"> Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, Ohio 44106</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Ohio</region>
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<wicri:cityArea> Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland</wicri:cityArea>
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<author><name sortKey="Berdis, Anthony J" sort="Berdis, Anthony J" uniqKey="Berdis A" first="Anthony J." last="Berdis">Anthony J. Berdis</name>
<affiliation wicri:level="2"><nlm:aff id="A2"> Department of Pharmacology, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, Ohio 44106</nlm:aff>
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<wicri:cityArea> Department of Pharmacology, Case Western Reserve University, 10900 Euclid Avenue, Cleveland</wicri:cityArea>
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<affiliation wicri:level="2"><nlm:aff id="A1"> Department of Chemistry, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, Ohio 44106</nlm:aff>
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<author><name sortKey="Berdis, Anthony J" sort="Berdis, Anthony J" uniqKey="Berdis A" first="Anthony J." last="Berdis">Anthony J. Berdis</name>
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<front><div type="abstract" xml:lang="en"><p id="P2">Nearly every DNA polymerase characterized to date exclusively catalyzes the incorporation of mononucleotides into a growing primer using a DNA or RNA template as a guide to direct each incorporation event. There is, however, one unique DNA polymerase designated terminal deoxynucleotidyl transferase that performs DNA synthesis using <italic>only</italic>
single-stranded DNA as the nucleic acid substrate. In this chapter, we review the biological role of this enigmatic DNA polymerase and the biochemical mechanism for its ability to perform DNA synthesis in the absence of a templating strand. We compare and contrast the molecular events for template-independent DNA synthesis catalyzed by terminal deoxynucleotidyl transferase with other well-characterized DNA polymerases that perform template-dependent synthesis. This includes a quantitative inspection of how terminal deoxynucleotidyl transferase binds DNA and dNTP substrates, the possible involvement of a conformational change that precedes phosphoryl transfer, and kinetic steps that are associated with the release of products. These enzymatic steps are discussed within the context of the available structures of terminal deoxynucleotidyl transferase in the presence of DNA or nucleotide substrate. In addition, we discuss the ability of proteins involved in replication and recombination to regulate the activity of the terminal deoxynucleotidyl transferase. Finally, the biomedical role of this specialized DNA polymerase is discussed focusing on its involvement in cancer development and its use in biomedical applications such as labeling DNA for detecting apoptosis.</p>
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