TY - JOUR
T1 - Identification and characterization of RAD9B, a paralog of the RAD9 checkpoint gene
AU - Dufault, Vanessa M.
AU - Oestreich, Andrea J.
AU - Vroman, Benjamin T.
AU - Karnitz, Larry M.
N1 - Funding Information:
We thank S. Kaufmann, J. Chen, and J. Sarkaria for thoughtful discussion and H. Hang for the generous gift of the HUS1B cDNA. We also thank Wanda Rhodes for expert secretarial assistance. This work was supported by NIH Grant CA84321 and the Mayo Clinic Foundation.
PY - 2003/12
Y1 - 2003/12
N2 - RAD9 is an integral element of the PCNA-like HUS1-RAD1-RAD9 (9-1-1) complex that participates in genotoxin-induced CHK1 activation. We have identified a novel RAD9 paralog, dubbed RAD9B, in humans and mice. RAD9 and RAD9B share extensive amino acid homology throughout their entire sequences (36% identity, 48% similarity). Northern blotting revealed that RAD9B transcripts are highly expressed in human testes, with lower levels found in skeletal muscle. In contrast, RT-PCR analysis and immunoprecipitation demonstrated that RAD9B is also expressed in tumor cells. Like RAD9, RAD9B associates with HUS1, RAD1, and RAD17, suggesting that it is a RAD9 paralog that engages in similar biochemical reactions. In addition, we have also shown that RAD9 and RAD9B interact with the HUS1 paralog, HUS1B. Taken together, these results suggest that these proteins can combinatorially assemble into distinct 9-1-1 clamps that may have distinct biological functions.
AB - RAD9 is an integral element of the PCNA-like HUS1-RAD1-RAD9 (9-1-1) complex that participates in genotoxin-induced CHK1 activation. We have identified a novel RAD9 paralog, dubbed RAD9B, in humans and mice. RAD9 and RAD9B share extensive amino acid homology throughout their entire sequences (36% identity, 48% similarity). Northern blotting revealed that RAD9B transcripts are highly expressed in human testes, with lower levels found in skeletal muscle. In contrast, RT-PCR analysis and immunoprecipitation demonstrated that RAD9B is also expressed in tumor cells. Like RAD9, RAD9B associates with HUS1, RAD1, and RAD17, suggesting that it is a RAD9 paralog that engages in similar biochemical reactions. In addition, we have also shown that RAD9 and RAD9B interact with the HUS1 paralog, HUS1B. Taken together, these results suggest that these proteins can combinatorially assemble into distinct 9-1-1 clamps that may have distinct biological functions.
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U2 - 10.1016/S0888-7543(03)00200-3
DO - 10.1016/S0888-7543(03)00200-3
M3 - Article
C2 - 14611806
AN - SCOPUS:0242678261
SN - 0888-7543
VL - 82
SP - 644
EP - 651
JO - Genomics
JF - Genomics
IS - 6
ER -