Nucleic Acids Research, Vol 26, Issue 16 3769-3775, Copyright © 1998 by Oxford University Press
JO Han, LA Erskine, MM Purugganan, TD Stamato and DB Roth
V(D)J recombination assembles immunoglobulin (Ig) and T cell receptor (TCR)
gene segments during lymphocyte development. Recombination is initiated by
the RAG-1 and RAG-2 proteins, which introduce double- stranded DNA breaks
(DSB) adjacent to the Ig and TCR gene segments. The broken ends are joined
by the DSB repair machinery, which includes the XRCC4 protein. While XRCC4
is essential for both DSB repair and V(D)J recombination, the functions of
this protein remain enigmatic. Because the rare V(D)J recombination
products isolated from XRCC4-deficient cells generally show evidence of
excessive nucleotide loss, it was hypothesized that XRCC4 may function to
protect broken DNA ends. Here we report the first examination of V(D)J
recombination intermediates in XRCC4-deficient cells. We found that both
types of intermediates, signal ends and coding ends, are abundant in the
absence of XRCC4. Furthermore, the signal ends are full length. We also
showed that alternative V(D)J recombination products, hybrid joints, form
with normal efficiency and without excessive deletion in XRCC4-deficient
cells. These data indicate that impaired formation of V(D)J recombination
products in XRCC4-deficient cells does not result from excessive
degradation of recombination intermediates. Potential roles of XRCC4 in the
joining reaction are discussed.
ARTICLES
V(D)J recombination intermediates and non-standard products in XRCC4- deficient cells
The Department of Microbiology and Immunology, Baylor College of Medicine and The Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030, USA.
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