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TdT interacting factor 1 enhances TdT ubiquitylation through recruitment of BPOZ‐2 into nucleus from cytoplasm
Author(s) -
Hayano Takahide,
Koiwai Kotaro,
Ishii Hisataka,
Maezawa So,
Kouda Kousuke,
Motoyama Takuro,
Kubota Takashi,
Koiwai Osamu
Publication year - 2009
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2009.01358.x
Subject(s) - biology , cytoplasm , nucleus , microbiology and biotechnology
We isolated human cDNA clone encoding Bood POZ containing gene type 2 (BPOZ‐2) as a gene with a product that binds to TdT interacting factor 1 (TdIF1) using a yeast two‐hybrid system. BPOZ‐2 is an adaptor for E3 ligase CUL3 and participates in developmental processes. The binding between BPOZ‐2 and TdIF1 was confirmed by GST pull‐down and immunoprecipitation assays using specific antibodies against BPOZ‐2 and TdIF1 in vitro and in vivo . Although when BPOZ‐2 solely was expressed in COS7 cells, BPOZ‐2 was observed mainly within the cytoplasm, co‐transfection of pEGFP‐BPOZ‐2 and pDsRed‐TdIF1 into COS7 cells resulted in co‐localization of EGFP‐BPOZ‐2 and DsRed‐TdIF1 within the nucleus. TdIF1 may recruit BPOZ‐2 into the nucleus from the cytoplasm by directly binding to BPOZ‐2. BPOZ‐2 enhanced TdT ubiquitylation when TdIF1 was expressed together with BPOZ‐2 in 293T cells, strongly suggesting that the recruitment of BPOZ‐2 into the nucleus from the cytoplasm is significant for the TdT ubiquitylation within the nucleus.