Distinct and opposite diversifying activities of terminal transferase splice variants

T. H. Thai; M. M. Purugganan; D. B. Roth; J. F. Kearney

doi:10.1038/ni788

Distinct and opposite diversifying activities of terminal transferase splice variants

T. H. Thai, M. M. Purugganan, D. B. Roth, J. F. Kearney

Research output: Contribution to journal › Article › peer-review

Abstract

The short splice variant of mouse terminal deoxynucleotidyl transferase (TdTS) catalyzes the addition of nontemplated nucleotides (N addition) at the coding joins of B cell and T cell antigen receptor genes. However, the activity and function of the long isoform of TdT (TdTL) have not been determined. We show here, in vitro and in vivo, that TdTL is a 3'-->5' exonuclease that catalyzes the deletion of nucleotides at coding joins. These findings suggest that the two TdT isoforms may act in concert to preserve the integrity of the variable region of antigen receptors while generating diversity.

Original language	Undefined
Pages (from-to)	457-62
Journal	Viral Immunology
Volume	3
Issue number	5
DOIs	https://doi.org/10.1038/ni788
State	Published - 2002

Keywords

Alternative Splicing/*immunology Amino Acid Motifs/immunology Amino Acid Sequence Animals Antigenic Variation/*immunology B-Lymphocytes/*enzymology Cyclin-Dependent Kinase Inhibitor p21 Cyclins/chemistry DNA Nucleotidylexotransferase/genetics/*immunology Isoenzymes/genetics/immunology Mice Mice, Transgenic Molecular Sequence Data RNA/chemistry/genetics Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid

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10.1038/ni788

Cite this

@article{8968227e846847f19c496b20fa3b6e95,

title = "Distinct and opposite diversifying activities of terminal transferase splice variants",

abstract = "The short splice variant of mouse terminal deoxynucleotidyl transferase (TdTS) catalyzes the addition of nontemplated nucleotides (N addition) at the coding joins of B cell and T cell antigen receptor genes. However, the activity and function of the long isoform of TdT (TdTL) have not been determined. We show here, in vitro and in vivo, that TdTL is a 3'-->5' exonuclease that catalyzes the deletion of nucleotides at coding joins. These findings suggest that the two TdT isoforms may act in concert to preserve the integrity of the variable region of antigen receptors while generating diversity.",

keywords = "Alternative Splicing/*immunology Amino Acid Motifs/immunology Amino Acid Sequence Animals Antigenic Variation/*immunology B-Lymphocytes/*enzymology Cyclin-Dependent Kinase Inhibitor p21 Cyclins/chemistry DNA Nucleotidylexotransferase/genetics/*immunology Isoenzymes/genetics/immunology Mice Mice, Transgenic Molecular Sequence Data RNA/chemistry/genetics Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid",

author = "Thai, {T. H.} and Purugganan, {M. M.} and Roth, {D. B.} and Kearney, {J. F.}",

note = "Thai, To-Ha Purugganan, Mary M Roth, David B Kearney, John F AI 07051/AI/NIAID NIH HHS/United States AI 523133/AI/NIAID NIH HHS/United States AI36420/AI/NIAID NIH HHS/United States R01 AI014782/AI/NIAID NIH HHS/United States T32 AI007051/AI/NIAID NIH HHS/United States Journal Article Research Support, U.S. Gov't, P.H.S. United States Nat Immunol. 2002 May;3(5):457-62. Epub 2002 Apr 8.",

year = "2002",

doi = "10.1038/ni788",

language = "Undefined",

volume = "3",

pages = "457--62",

journal = "Viral Immunology",

issn = "0882-8245",

publisher = "Mary Ann Liebert Inc.",

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TY - JOUR

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AU - Thai, T. H.

AU - Purugganan, M. M.

AU - Roth, D. B.

AU - Kearney, J. F.

N1 - Thai, To-Ha Purugganan, Mary M Roth, David B Kearney, John F AI 07051/AI/NIAID NIH HHS/United States AI 523133/AI/NIAID NIH HHS/United States AI36420/AI/NIAID NIH HHS/United States R01 AI014782/AI/NIAID NIH HHS/United States T32 AI007051/AI/NIAID NIH HHS/United States Journal Article Research Support, U.S. Gov't, P.H.S. United States Nat Immunol. 2002 May;3(5):457-62. Epub 2002 Apr 8.

PY - 2002

Y1 - 2002

N2 - The short splice variant of mouse terminal deoxynucleotidyl transferase (TdTS) catalyzes the addition of nontemplated nucleotides (N addition) at the coding joins of B cell and T cell antigen receptor genes. However, the activity and function of the long isoform of TdT (TdTL) have not been determined. We show here, in vitro and in vivo, that TdTL is a 3'-->5' exonuclease that catalyzes the deletion of nucleotides at coding joins. These findings suggest that the two TdT isoforms may act in concert to preserve the integrity of the variable region of antigen receptors while generating diversity.

AB - The short splice variant of mouse terminal deoxynucleotidyl transferase (TdTS) catalyzes the addition of nontemplated nucleotides (N addition) at the coding joins of B cell and T cell antigen receptor genes. However, the activity and function of the long isoform of TdT (TdTL) have not been determined. We show here, in vitro and in vivo, that TdTL is a 3'-->5' exonuclease that catalyzes the deletion of nucleotides at coding joins. These findings suggest that the two TdT isoforms may act in concert to preserve the integrity of the variable region of antigen receptors while generating diversity.

KW - Alternative Splicing/immunology Amino Acid Motifs/immunology Amino Acid Sequence Animals Antigenic Variation/immunology B-Lymphocytes/enzymology Cyclin-Dependent Kinase Inhibitor p21 Cyclins/chemistry DNA Nucleotidylexotransferase/genetics/immunology Isoe

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