@article{,
title = {Critical residues for RNA discrimination of the histone hairpin binding protein (HBP) investigated by the yeast three-hybrid system},
author = {S Jaeger and G Eriani and F Martin},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14706861},
isbn = {14706861},
year = {2004},
date = {2004-01-01},
journal = {FEBS Lett},
volume = {556},
number = {1-3},
pages = {265-270},
abstract = {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.},
note = {0014-5793
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Amino Acid Substitution Base Sequence Carrier Proteins/chemistry/*genetics/*metabolism Histones/genetics Human Lac Operon/genetics Molecular Sequence Data Nucleic Acid Conformation Nucleotides/chemistry/genetics/metabolism RNA/chemistry/genetics/*metabolism RNA, ERIANI, Messenger/chemistry/genetics/metabolism RNA-Binding Proteins/chemistry/genetics/metabolism Recombinant Fusion Proteins/chemistry/genetics/metabolism Saccharomyces cerevisiae/*genetics Sequence Alignment Sequence Homology, Non-U.S. Gov't Two-Hybrid System Techniques beta-Galactosidase/genetics/metabolism, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.