Recombination of protein domains facilitated by co-translational folding in eukaryotes (original) (raw)
References
Gilbert, W. The exon theory of genes. Cold Spring Harb. Symp. Quant. Biol.LII, 901–905 (1987). Article Google Scholar
Blake, C. C. F. Exons and the evolution of proteins. Int. Rev. Cytol.93, 149–185 (1985). ArticleCAS Google Scholar
Doolittle, R. F. & Bork, P. Evolutionary mobile modules in proteins. Sci. Am.269, 50–56 ((1993)). ArticleCAS Google Scholar
Stolzfus, A., Spencer, D. F., Zuker, M., Logsdon, J. M. & Doolittle, W. F. Testing the exon theory of genes: The evidence from protein structure. Science265, 202–207 (1994). ArticleADS Google Scholar
Richardson, J. S. Describing patterns of protein tertiary structure. Methods Enzymol.115, 341–380 (1985). ArticleADSCAS Google Scholar
Doolittle, RF. The multiplicity of domains in proteins. Annu. Rev. Biochem.64, 287–314 (1995). ArticleCAS Google Scholar
Orengo, C. A., Jones, D. T. & Thornton, J. M. Protein superfamilies and domain superfolds. Nature372, 631–634 (1994). ArticleADSCAS Google Scholar
Jaenicke, R. Folding and association of proteins. Prog. Biophys. Mol. Biol.49, 117–237 (1987). ArticleCAS Google Scholar
Marston, F. A. O. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J.240, 1–12 (1986). ArticleCAS Google Scholar
Hartl, F. U. Molecular chaperones in cellular protein folding. Nature381, 571–580 (1996). ArticleADSCAS Google Scholar
Kubota, H., Hynes, G. & Willison, K. The chaperonin containing t-complex polypeptide 1 (TCP-1)—Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur. J. Biochem.230, 3–16 (1995). ArticleCAS Google Scholar
Lewis, S. A., Tian, G. L., Vainberg, I. E. & Cowan, N. J. Chaperonin-mediated folding of actin and tubulin. J. Cell Biol.132, 1–4 (1996). ArticleCAS Google Scholar
Weissman, J. S. & Kim, P. The Pro region of BPTI facilitates folding. Cell71, 841–851 (1992). ArticleCAS Google Scholar
Stewart, M. L., Grollman, A. P. & Huang, M. -T. Aurintricarboxylic acid: Inhibitor of initiation of protein synthesis. Proc. Natl Acad. Sci. USA68, 97–101 (1971). ArticleADSCAS Google Scholar
Frydman, J., Nimmesgern, E., Ohtsuka, K. & Hartl, F. U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature370, 111–117 (1994). ArticleADSCAS Google Scholar
Gesteland, R. F. Unfolding of Escherichia coli ribosomes by removal of magnesium. J. Mol. Biol.18, 356–371 (1966). ArticleCAS Google Scholar
Martin, J. et al. Chaperonin-mediated protein folding at the surface of groEL through a ‘molten globule’-like intermediate. Nature352, 36–42 (1991). ArticleADSCAS Google Scholar
Kenney, L. J., Bauer, M. D. & Silhavy, T. J. Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli.Proc. Natl Acad. Sci. USA92, 8866–8870 (1995). ArticleADSCAS Google Scholar
Martinez-Hackert, E. & Stock, A. M. The DNA-binding domain of OmpR: crystal structure of a winged helix transcription factor. Structure5, 109–124 (1997). ArticleCAS Google Scholar
Chotia, C. One thousand families for the molecular biologist. Nature357, 543–544 (1992). ArticleADS Google Scholar
Bergman, L. W. & Kuehl, W. M. Formation of an intrachain disulfide bond on nascent immunoglobulin. J. Biol. Chem.254, 8869–8876 (1979). CASPubMed Google Scholar
Chen, W., Helenius, J., Braakman, I. & Helenius, A. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl Acad. Sci. USA92, 6229–6233 (1995). ArticleADSCAS Google Scholar
Kolb, V. A., Makeyev, E. V. & Spirin, A. S. Folding of firefly luciferase during translation in a cell-free system. EMBO J.13, 3631–3637 (1994). ArticleCAS Google Scholar
Gaitanaris, G. A., Vysokanov, A., Hung, S. -Z., Gottesman, M. & Gragerov, A. Successive action of E. coli chaperones in vivo. Mol. Microbiol.14, 861–869 (1994). ArticleCAS Google Scholar
Bremer, H. & Dennis, P. P. in Escherichia coli and Salmonella: Cellular and Molecular Biology(ed. Neidhardt, F. C.) 1553–1569 (ASM, Washington DC, (1996)). Google Scholar
LaVallie, E. R. & McCoy, J. M. Gene fusion expression systems in Escherichia coli.Curr. Opin. Biotechnol.6, 501–506 (1995). ArticleCAS Google Scholar
Sharrocks, A. D. AT7 expression vector for producing N- and C-terminal fusion proteins with glutathioone S-transferase. Gene138, 105–108 (1994). ArticleCAS Google Scholar
Hawkins, A. R. & Lamb, H. K. The molecular biology of multidomain proteins. Selected examples. Eur. J. Biochem.232, 7–18 (1995). ArticleCAS Google Scholar
Horwich, A. L., Low, K. B., Fenton, W. A., Hirschfield, I. N. & Furtak, K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell74, 909–917 (1993). ArticleCAS Google Scholar
Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. & Holmes, K. C. Atomic structure of the actin: DNAse I complex. Nature347, 37–44 (1990). ArticleADSCAS Google Scholar
Beckmann, R. P., Mizzen, L. A. & Welch, W. J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science248, 850–854 (1990). ArticleADSCAS Google Scholar
Nelson, R. J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M. & Craig, E. A. The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell71, 97–105 (1993). Article Google Scholar
Mayhew, M. et al. Protein folding in the central cavity of the GroEL–GroES chaperonin complex. Nature379, 420–426 (1996). ArticleADSCAS Google Scholar
Feuerstein, J., Goody, R. S. & Wittinghofer, A. Properties and characterization of nucleotide-free and metal ion-free p21 “Apoprotein”. J. Biol. Chem.262, 8455–8458 (1987). CASPubMed Google Scholar
Pratt, J. M. in Transcription and Translation: A Practical Approach(eds Hames, B. D. & Higgins, S. J.) 179–210 (IRL, Oxford, (1984)). Google Scholar
Cameau, D. E., Ikenaka, K., Tsung, K. L. & Inouye, M. Primary characterization of the protein products of the Escherichia coli ompB locus: structure and regulation of synthesis of the OmpR and EnvZ proteins. J. Bacteriol.164, 578–584 (1985). Google Scholar
Felgner, P. L. et al. Lipofection: a highly efficient, lipid-mediated DNA-transfection procedure. Proc. Natl Acad. Sci. USA84, 7413–7417 (1987). ArticleADSCAS Google Scholar
Ausubel, F. M. et al. Current Protocols in Molecular Biology pp. 6.11.5 (Wiley, New York, (1993). Google Scholar
Tucker, J. et al. Expression of p21 proteins in Escherichia coli and stereochemistry of th nucleotide-binding site. EMBO J.5, 1351–1358 (1986). ArticleCAS Google Scholar