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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Base Sequence
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Carrier Proteins / chemistry
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Carrier Proteins / genetics*
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Carrier Proteins / metabolism*
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Chromosomal Proteins, Non-Histone*
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Histones / genetics
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Humans
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Lac Operon / genetics
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Molecular Sequence Data
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Nucleic Acid Conformation
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Nucleotides / chemistry
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Nucleotides / genetics
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Nucleotides / metabolism
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RNA / chemistry
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RNA / genetics
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RNA / metabolism*
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RNA, Messenger / chemistry
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae / genetics*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Two-Hybrid System Techniques
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beta-Galactosidase / genetics
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beta-Galactosidase / metabolism
Substances
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Carrier Proteins
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Chromosomal Proteins, Non-Histone
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Histones
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Nucleotides
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RNA, Messenger
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RNA-Binding Proteins
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Recombinant Fusion Proteins
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RNA
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beta-Galactosidase