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The DNA binding activity of Translin is mediated by a basic region in the ring‐shaped structure conserved in evolution
Author(s) -
Aoki Katsunori,
Suzuki Kenji,
Ishida Reiko,
Kasai Masataka
Publication year - 1999
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(99)00010-1
Subject(s) - leucine zipper , dna , point mutation , hmg box , dna binding site , biology , bzip domain , binding site , dna binding domain , dna binding protein , microbiology and biotechnology , binding domain , mutation , genetics , biochemistry , gene , peptide sequence , transcription factor , promoter , gene expression
DNA binding proteins, for the most part, function as dimers or tetramers which recognize their target sequences. Here we show that Translin, a novel single‐stranded DNA end binding protein, forms a ring‐shaped structure conserved throughout evolution and that this structure is responsible for its DNA binding activity. Point mutations at Leu 184 and Leu 191 in the leucine zipper motif of human Translin resulted in loss of the multimeric structure and abrogation of DNA binding. Point mutations at R 86 , H 88 , H 90 to T 86 , N 88 , N 90 in one of the basic regions, however, completely inhibited the DNA binding activity without affecting the multimeric structure. These results support the view that the DNA binding domain of Translin is formed in the ring‐shaped structure in combination with its basic region (amino acids 86–97) polypeptides.