PMID:9867837
| Citation |
Korber, P, Zander, T, Herschlag, D and Bardwell, JC (1999) A new heat shock protein that binds nucleic acids. J. Biol. Chem. 274:249-56 |
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| Abstract |
We describe the isolation of Hsp15, a new, very abundant heat shock protein that binds to DNA and RNA. Hsp15 is well conserved and related to a number of RNA-binding proteins, including ribosomal protein S4, RNA pseudouridine synthase, and tyrosyl-tRNA synthetase. The region shared between these proteins appears to represent a common, but previously unrecognized, RNA binding motif. Filter binding studies showed that Hsp15 binds to a 17-mer single-stranded RNA with a dissociation constant of 9 microM in 22.5 mM Hepes, pH 7. 0, 5 mM MgCl2. A role of Hsp15 in binding nucleic acids puts this protein into a different functional category from that of many other heat shock proteins that act as molecular chaperones or proteases on protein substrates. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Chromatography, Affinity; Cloning, Molecular; Conserved Sequence; DNA/metabolism; DNA Primers; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Molecular Sequence Data; Protein Binding; RNA/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; Sequence Homology, Amino Acid |
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