TY - JOUR
T1 - V(D)J recombination signal recognition
T2 - Distinct, overlapping DNA- protein contacts in complexes containing RAG1 with and without RAG2
AU - Swanson, Patrick C.
AU - Desiderio, Stephen
N1 - Funding Information:
We thank Joanne Hesse, Dik van Gent, and Martin Gellert for reagents, Randy Mann for helpful discussions, and the Howard Hughes Medical Institute Biopolymers Facility at Johns Hopkins (Clark Riley, Director) for oligonucleotides. Nick Dordai provided expert technical assistance. This work was supported by the Howard Hughes Medical Institute and by grant CA16519 from the National Cancer Institute. P. C. S. is an Associate of the Howard Hughes Medical Institute.
PY - 1998/7
Y1 - 1998/7
N2 - Protein interactions with V(D)J recombination signal sequences (RSSs) were mapped in complexes containing RAG1 with (M1/2) or without (M1) RAG2. In both complexes, RAG interactions with the DNA backbone are biased toward one side of the helix; nonamer contacts resemble those of Hin with hixL. In the M1 complex, DNA contacts are centered on the nonamer. In the M1/2 complex, protein-RSS interactions extend through the spacer and into the nonamer- proximal portion of the heptamer. Chemical modifications near the heptamer- coding junction are overrepresented in the M1/2 complex, providing evidence for perturbation of DNA structure in this region. Thus, while RAG1 alone can bind the nonamer, RAG2 is required for heptamer occupancy.
AB - Protein interactions with V(D)J recombination signal sequences (RSSs) were mapped in complexes containing RAG1 with (M1/2) or without (M1) RAG2. In both complexes, RAG interactions with the DNA backbone are biased toward one side of the helix; nonamer contacts resemble those of Hin with hixL. In the M1 complex, DNA contacts are centered on the nonamer. In the M1/2 complex, protein-RSS interactions extend through the spacer and into the nonamer- proximal portion of the heptamer. Chemical modifications near the heptamer- coding junction are overrepresented in the M1/2 complex, providing evidence for perturbation of DNA structure in this region. Thus, while RAG1 alone can bind the nonamer, RAG2 is required for heptamer occupancy.
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U2 - 10.1016/S1074-7613(00)80593-2
DO - 10.1016/S1074-7613(00)80593-2
M3 - Article
C2 - 9697841
AN - SCOPUS:0032126295
SN - 1074-7613
VL - 9
SP - 115
EP - 125
JO - Immunity
JF - Immunity
IS - 1
ER -