Terminal deoxynucleotidyl transferases from elasmobranchs reveal structural conservation within vertebrates

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Bartl, S., Miracle, A. L., Rumfelt, L. L., Kepler, T. B., Mochon, E., Litman, G. W., & Flajnik, M. F. (2003). Terminal deoxynucleotidyl transferases from elasmobranchs reveal structural conservation within vertebrates. Immunogenetics, 55(9), 594-604. doi:10.1007/s00251-003-0608-3
Metadata
TitleTerminal deoxynucleotidyl transferases from elasmobranchs reveal structural conservation within vertebrates
AuthorsS. Bartl, A. Miracle, L. Rumfelt, T. Kepler, E. Mochon, G. Litman, M. Flajnik
AbstractThe DNA polymerase (pol) X family is an ancient group of enzymes that function in DNA replication and repair (pol β), translesion synthesis (pol λ and pol μ) and terminal addition of non-templated nucleotides. This latter terminal deoxynucleotidyl transferase (TdT) activity performs the unique function of providing diversity at coding joins of immunoglobulin and T-cell receptor genes. The first isolated full-length TdT genes from shark and skate are reported here. Comparisons with the three-dimensional structure of mouse TdT indicate structural similarity with elasmobranch orthologues that supports both a template-independent mode of replication and a lack of strong nucleotide bias. The vertebrate TdTs appear more closely related to pol μ and fungal polymerases than to pol λ and pol β. Thus, unlike other molecules of adaptive immunity, TdT is a member of an ancient gene family with a clear gene phylogeny and a high degree of similarity, which implies the existence of TdT ancestors in jawless fishes and invertebrates.
JournalImmunogenetics
Date2003
Volume55
Issue9
Start page594
End page604
ISSN0093-7711
SubjectsDNA nucleotidylexotransferase, DNA polymerase, fungal enzyme, immunoglobulin, T lymphocyte receptor, article, DNA structure, Elasmobranchii, electric fish, enzyme activity, enzyme structure, gene function, gene isolation, gene replication, genetic code, genetic conservation, genetic variability, human, immunity, multigene family, nonhuman, phylogeny, priority journal, protein function, shark, terminal sequence, vertebrate, Amino Acid Sequence, Animals, Conserved Sequence, DNA-Directed DNA Polymerase, Evolution, Mice, Molecular Sequence Data, Protein Conformation, Protein Folding, Sequence Homology, Amino Acid, Agnatha, Chondrichthyes, Ginglymostoma cirratum, Invertebrata, Pisces, Raja eglanteria, Vertebrata
NoteCited By (since 1996):10, Fish and Fisheries, CODEN: IMNGB

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