The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG‐ and CCAAT sequences in single stranded oligonucleotides

FEBS Letters

Graumann, Peter¹  Marahiel, Mohamed A.¹ 

[1] Biochemie, Fachbereich Chemie, Hans Meerwein Straße, Philipps Universität Marburg, 35032 Marburg, Germany

关键词: Cold shock protein;    CspB;    Cold shock domain (CSD);    Y-box sequence;    B. subtilis;   

DOI  :  10.1016/0014-5793(94)80355-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have characterized the nucleic acid binding properties of the major cold shock protein of Bacillus subtilis, CspB. CspB is a member of the cold shock domain (CSD) family, which is widespread among pro- and eukaryotes and shares the nucleic acid binding domain CSD. The CSD domain is highly conserved and binds with strong affinity to the Y-box motif, a cis-element that contains the CTG AA sequence. In a series of gel retardation experiments using oligonucleotides, which contain the Y-box motif and altered sequences, we show the preferential binding of CspB to single-stranded DNA that contains the ATTGG as well as the complementary CCAAT Y-box core sequence. In contrast CspB exhibits lower affinity to altered Y-box core sequences. Dependent on the length of the oligonucleotide and the degree of sequence deviation from the Y-box core sequence 3- to over 10-fold overexcess of CspB was needed for complete retardation.

【 授权许可】

Unknown