Members of the 70-Kilodalton Heat Shock Protein Family Contain a Highly Conserved Calmodulin-Binding Domain

Literature Cited

• Bardwell, J. C., and E. A. Craig. 1984. Major heat shock genes of Drosophila and Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. USA 81:848–852.
   PubMed Web of Science ®Google Scholar
• Billingsley, M. L., K. R. Pennypacker, C. G. Hoover, D. J. Brigati, and R. L. Kincaid. 1985. A rapid and sensitive method for detection of calcineurin and calmodulin binding proteins using biotinylated calmodulin. Proc. Natl. Acad. Sci. USA 82:7585–7589.
   PubMedGoogle Scholar
• Blumenthal, D. K., K. Takio, A. M. Edelman, H. Charbonneau, K. Titani, K. A. Walsh, and E. G. Krebs. 1985. Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proc. Natl. Acad. Sci. USA 82:3187–3191.
   PubMed Web of Science ®Google Scholar
• Chappell, T. G., W. J. Welch, D. M. Schlossman, K. B. Palter, M. J. Schlesinger, and J. E. Rothman. 1986. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. Cell 45:3–13.
   PubMed Web of Science ®Google Scholar
• Chirico, W. J., M. G. Waters, and G. Blobel. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature (London) 332:805–810.
   PubMed Web of Science ®Google Scholar
• Chou, P. Y., and G. D. Fasman. 1978. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47:45–148.
   PubMedGoogle Scholar
• Clark, B. D., and I. R. Brown. 1986. A retinal heat-shock protein is associated with elements of the cytoskeleton and binds to calmodulin. Biochem. Biophys. Res. Commun. 139:974–981.
   PubMedGoogle Scholar
• Comte, Μ., Y. Maulet, and J. A. Cox. 1983. Ca2+ dependent high-affinity complex formation between calmodulin and melittin. Biochem. J. 209:269–272.
   PubMedGoogle Scholar
• DeGrado, W. F., F. G. Predergast, H. R. Wolfe, and J. H. Cox. 1985. The design, synthesis and characterization of tight-binding inhibitors of calmodulin. J. Cell. Biochem. 29:83–93.
   PubMedGoogle Scholar
• Deshaies, R. J., B. D. Koch, M. Werner-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature (London) 332:800–805.
   PubMed Web of Science ®Google Scholar
• Drummond, I. A. S., S. A. McClure, M. Poenie, R. Y. Tsien, and R. A. Steinhardt. 1986. Large changes in intracellular pH and calcium observed during heat shock are not responsible for the induction of heat shock proteins in Drosophila melanogaster. Mol. Cell. Biol. 6:1767–1775.
   PubMed Web of Science ®Google Scholar
• Giebel, L. B., B. P. Dworniczak, and E. K. F. Bautz. 1988. Developmental regulation of a constitutively expressed mouse mRNA encoding a 72-kDa heat shock-like protein. Dev. Biol. 125:200–207.
   PubMed Web of Science ®Google Scholar
• Guerriero, V., M. A. Russo, N. J. Olson, J. A. Putkey, and A. R. Means. 1986. Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNA. Biochemistry 25:8372–8381.
   PubMedGoogle Scholar
• Hanley, R. M., A. M. Means, B. E. Kemp, and S. Shenolikar. 1988. Mapping of calmodulin-binding domain of Ca2+/calmodu- lin dependent protein kinase II. Biochem. Biophys. Res. Commun. 152:122–128.
   PubMedGoogle Scholar
• Hinds, P. W., C. A. Finlay, A. B. Frey, and A. J. Levine. 1987. Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines. Mol. Cell. Biol. 7:2863–2869.
   PubMed Web of Science ®Google Scholar
• Hughes, E. N., and J. T. August. 1982. Co-precipitation of heat shock proteins with a cell surface glycoprotein. Proc. Natl. Acad. Sci. USA 79:2305–2309.
   PubMed Web of Science ®Google Scholar
• Hunt, C., and R. I. Morimoto. 1985. Conserved features of eucaryotic hsp 70 genes revealed by comparison with the nucleotide sequences of human hsp 70. Proc. Natl. Acad. Sci. USA 82:6455–6459.
   PubMed Web of Science ®Google Scholar
• Ingolia, T. D., E. A. Craig, and B. J. McCarthy. 1980. Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions. Cell 21:669–679.
   PubMed Web of Science ®Google Scholar
• Ingolia, T., M. R. Slater, and E. A. Craig. 1982. Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila. Mol. Cell. Biol. 2:1388–1398.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• Lewis, M. J., and H. R. B. Pelham. 1985. Involvement of ATP in the nuclear and nucleolar functions of the 70 kd heat shock protein. EMBO J. 4:3137–3143.
   PubMed Web of Science ®Google Scholar
• Lucas, T. J., W. H. Burgess, F. G. Predergast, W. Lau, and D. M. Watterson. 1986. Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase. Biochemistry 25:1458–1464.
   PubMedGoogle Scholar
• Milarski, K. L., W. J. Welch, and R. I. Morimoto. 1989. Cell cycle-dependent association of HSP70 with specific cellular proteins. J. Cell Biol. 108:413–423.
   PubMed Web of Science ®Google Scholar
• Munro, S., and H. R. B. Pelham. 1984. Use of peptide tagging to detect proteins expressed from cloned genes: deletion mapping functional domains of Drosophila hsp 70. EMBO J. 3:3087–3093.
   PubMed Web of Science ®Google Scholar
• O'Malley, K., A. Mauron, J. D. Barchas, and L. Kedes. 1985. Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein. Mol. Cell. Biol. 5:3476–3483.
   PubMedGoogle Scholar
• Pearson, R. B., R. E. H. Wettenhall, A. R. Means, D. J. Hartshorne, and B. E. Kemp. 1988. Autoregulation of enzymes by pseudosubstrate prototypes: myosin light chain kinase. Science 241:970–973.
   PubMedGoogle Scholar
• Stevenson, M. A., S. K. Calderwood, and G. M. Hahn. 1986. Rapid increases in inositol trisphosphate and intracellular Ca++ after heat shock. Biochem. Biophys. Res. Commun. 137:826–833.
   PubMed Web of Science ®Google Scholar
• Ting, J., and A. S. Lee. 1988. Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation and regulation. DNA 7:275–286.
   PubMedGoogle Scholar
• Towbin, Η., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350–4354.
   PubMed Web of Science ®Google Scholar
• Wallace, R. W., E. A. Tailant, and W. Y. Cheung. 1983. Assay of calmodulin by Ca2+-dependent phosphodiesterase. Methods Enzymol. 102:39–47.
   PubMed Web of Science ®Google Scholar
• Wang, C., D. J. Asai, and E. Lazarides. 1980. The 68,000-dalton neurofilament-associated polypeptide is a component of nonneuronal cell and of skeletal myofibrils. Proc. Natl. Acad. Sci. USA 77:1541–1545.
   PubMed Web of Science ®Google Scholar
• Welch, W. J., and J. R. Feramisco. 1985. Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides. Mol. Cell. Biol. 5:1229–1237.
   PubMed Web of Science ®Google Scholar
• Whatley, S. A., T. Leung, C. Hall, and L. Lim. 1986. The brain 68-kilodalton microtubule-associated protein is the cognate form of the 70-kilodalton mammalian heat-shock protein and is present as a specific isoform in synaptosomal membranes. J. Neurochem. 47:1576–1583.
   PubMedGoogle Scholar
• Zakeri, Z. F., D. J. Wolgemuth, and C. Hunt. 1988. Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line. Mol. Cell. Biol. 8:2925–2932.
   PubMed Web of Science ®Google Scholar
• Zimmerman, R., M. Sagstetter, M. J. Lewis, and H. R. B. Pelham. 1988. Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes. EMBO J. 7:2875–2880.
   PubMedGoogle Scholar