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Okamoto, N.* ; Okamoto, M.* ; Araki, S.* ; Arakawa, H. ; Mizuta, R.* ; Kitamura, D.*

Possible contribution of DNase γ to immunoglobulin V gene diversification.

Immunol. Lett. 125, 22-30 (2009)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Somatic hypermutation (SHM) diversifies the rearranged immunoglobulin variable (V) region gene in B cells, contributing to affinity maturation of antibodies. It is believed that SHM is generated either by direct replication or by error-prone repair systems resolving V region DNA lesions caused directly or indirectly by cytidine deaminase AID. In accord with a part of these mechanisms, it was reported that SHM is associated with staggered double-strand DNA breaks (DSBs) occurring in the rearranged V regions. However, endonucleases responsible for the DSBs remain elusive. Here we show that DNase gamma, a member of DNase I family endonucleases, contributes to the generation of SHM including point mutation, and nucleotide insertion and deletion in chicken DT40 B cell line. DNase gamma also contributes to the generation of staggered DSBs in the rearranged V region. These results raise a possibility that DNase gamma is involved in the V gene mutation machinery.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Somatic hypermutation; Immunoglobulin variable region; Double-strand DNA breaks; Endonucleases; DNase gamma; class switch recombination; single-stranded-dna; cytidine deaminase aid; somatic hypermutation; cell-line; homologous recombination; antibody diversity; breaks; conversion; translocations
Sprache englisch
Veröffentlichungsjahr 2009
HGF-Berichtsjahr 2009
ISSN (print) / ISBN 0165-2478
e-ISSN 1879-0542
Zeitschrift Immunology Letters
Quellenangaben Band: 125, Heft: 1, Seiten: 22-30 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Radiation Biology (IMS)
PSP-Element(e) G-500400-001
Scopus ID 67649992296
PubMed ID 19501119
Erfassungsdatum 2009-12-31