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Critical residues for RNA discrimination of the histone hairpin binding protein (HBP) investigated by the yeast three‐hybrid system
Author(s) -
Jaeger Sophie,
Eriani Gilbert,
Martin Franck
Publication year - 2004
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(03)01433-9
Subject(s) - histone , yeast , stem loop , microbiology and biotechnology , biology , rna , rna binding protein , small hairpin rna , chemistry , binding domain , biochemistry , binding site , gene
The histone hairpin binding protein (HBP, also called SLBP, which stands for stem‐loop binding protein) binds specifically to a highly conserved hairpin structure located in the 3′ UTR of the cell‐cycle‐dependent histone mRNAs. HBP consists of a minimal central RNA binding domain (RBD) flanked by an N‐ and C‐terminal domain. The yeast three‐hybrid system has been used to investigate the critical residues of the human HBP involved in the binding of its target hairpin structure. By means of negative selections followed by positive selections, we isolated mutant HBP species. Our results indicate tight relationships between the RBD and the N‐ and C‐terminal domains.