DETERMINATION OF THE DNA-SEQUENCE RECOGNIZED BY THE BHLH-ZIP DOMAIN OF THE N-MYC PROTEIN

被引：55

作者：

ALEX, R ^{[1
]}

SOZERI, O ^{[1
]}

MEYER, S ^{[1
]}

DILDROP, R ^{[1
]}

机构：

[1] UNIV COLOGNE, INST GENET, WEYERTAL 121, W-5000 COLOGNE 41, GERMANY

来源：

NUCLEIC ACIDS RESEARCH | 1992年 / 20卷 / 09期

关键词：

D O I：

10.1093/nar/20.9.2257

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The DNA-binding domain of the murine N-Myc protein, comprising the basic helix-loop-helix-zipper (bHLH-zip) region was expressed as a fusion protein in E. coli. The affinity purified glutathione-S-transferase-N-Myc fusion protein (GST-N-MYC) was used to select the N-Myc specific DNA-recognition motif from a pool of random-sequence oligonucleotides. After seven rounds of binding-site selection, specifically enriched oligonucleotides were cloned and sequenced. Of 31 individual oligonucleotides whose sequences were determined, 30 contained a common DNA-motif, defining the hexameric consensus sequence CACGTG. We confirm by mutational analysis that binding of the N-Myc derived bHLH-zip domain to this motif is sequence-specific.

引用

页码：2257 / 2263

页数：7

共 35 条

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