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The human S mu bp-2, a DNA-binding protein specific to the single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region

Authors :
Akira Shimizu
Tatsunobu-Ryushin Mizuta
Tasuku Honjo
Yosho Fukita
Kazuo Ozawa
M Shirozu
Source :
The Journal of biological chemistry. 268(23)
Publication Year :
1993

Abstract

We have cloned the cDNA encoding the human homologue of S mu bp-2, which binds to single-stranded DNA with 5'-phosphorylated guanine-rich sequences related to the immunoglobulin mu chain switch (S mu) region. The deduced amino acid sequences of the mouse and human S mu bp-2 are 76.5% homologous and contain motifs conserved among helicases. We have identified a domain essential for DNA binding at residues 638-786. The binding domain is less conserved (63% homologous) than the putative catalytic domain of N-terminal half containing most of the helicase motifs (85% homologous). The human and mouse S mu bp-2 have similar, although slightly different, binding specificities. Although the mouse S mu bp-2 preferentially binds to the mouse S mu motif (GGGGT), the human S mu bp-2 binds equally well to the human (GGGCT) and mouse S mu motifs. The human S mu bp-2 gene was mapped to chromosome 11 q13.2-q13.4 by in situ hybridization.

Details

ISSN :
00219258
Volume :
268
Issue :
23
Database :
OpenAIRE
Journal :
The Journal of biological chemistry
Accession number :
edsair.doi.dedup.....0e3cadc907d8ba09d46df724627a5909