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Papers In Press, published online ahead of print October 21, 2003
Department of Biology, Chiba University, Faculty of Science, Chiba 263-8522
Corresponding Author: tamura{at}bio.s.chiba-u.ac.jp
SUMMARY TBP-like protein (TLP) is structurally similar to TBP and is thought to have a transcriptional regulation function. Although TLP has been found to form a complex with TFIIA, the in vivo functions of TFIIA for TLP are not clear. In this study, we analyzed in detail the interaction between TLP and TFIIA. Dissociation constants of TFIIA vs. TLP and TFIIA vs. TBP were 1.5 nM and 10 nM, respectively. The dissociation rate constant of TLP and TFIIA (1.2 x 10-4/M.sec) was lower than that of TBP (2.1 x 10-3/M.sec). These results indicate that TLP has a higher affinity to TFIIA than does TBP. We found that TLP forms a dimer and a trimer and that these multimerizations are inhibited by TFIIA. TLP mutimers were more stable than a TBP dimer. We found that the molecular number of TLP in the nucleus was only 2% of that in the cytoplasm of HeLa cells. Immunostaining of cells also revealed cytoplasmic localization of TLP. We established cells that stably express TLP and identified amino acids of TLP required for TFIIA binding (A32, L33, N37, R52, K53, R86). We investigated the effect of those amino acid substitutions on the cytoplasmic localization of TLP. Interestingly, the level of the TFIIA-binding-defective mutant TLPs in the nucleus was much higher than that of the wild-type TLP and TFIIA-interactable mutant TLPs. Immunostaining analyses showed consistent results. These results suggest that the TFIIA-binding ability of TLP is required for characteristic cytoplasmic localization of TLP.
J. Biol. Chem, 10.1074/jbc.M305412200
Submitted on May 23, 2003
Revised on October 21, 2003
Accepted on October 17, 2003
Specific interaction with TFIIA and localization of the mammalian TBP-like protein (TLP/TRF2/TLF)
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