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FEBS Lett. 2004 Jan 2;556(1-3):265-70.

Critical residues for RNA discrimination of the histone hairpin binding protein (HBP) investigated by the yeast three-hybrid system.

Author information

1
Institut de Biologie Moléculaire et Cellulaire, UPR No. 9002 du CNRS, 15 rue René Descartes, 67084 Cedex, Strasbourg, France.

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.

PMID:
14706861
DOI:
10.1016/s0014-5793(03)01433-9
[Indexed for MEDLINE]
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