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Interaction of Oct‐1 and automodification domain of poly(ADP‐ribose) synthetase
Author(s) -
Nie Jing,
Sakamoto Shuji,
Song Demao,
Qu Zhiqiang,
Ota Katsuya,
Taniguchi Taketoshi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00131-8
Subject(s) - fusion protein , histone octamer , microbiology and biotechnology , complementary dna , dna , sequence motif , biology , western blot , pou domain , biochemistry , recombinant dna , transcription factor , gene , homeobox , nucleosome , histone
We isolated several clones from a matchmaker two‐hybrid system human lymphocyte cDNA library using an automodification domain of poly(ADP‐ribose) synthetase (PARS) as a probe. A DNA sequence (∼1 kbp) of the clone was identical to part of the Oct‐1 DNA sequence. We then constructed either a His‐tagged or GST fusion protein of the inserted cDNA from the clone and the fusion protein was shown to interact with PARS by far‐Western blot analysis and co‐precipitation with affinity resin. Furthermore, the His‐tagged Oct‐1/POU‐homeo fusion protein interacted weakly with the octamer motif of the DRa promoter and the addition of PARS fusion protein greatly increased the DNA binding activity. These results suggest that PARS interacts with Oct‐1 and stabilizes the binding of Oct‐1 to the octamer motif.