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Ents was preceded or accompanied by duplication of the genes for the chaperone proteins (Hsp70, Hsp90, DnaJ, etc.), which are necessary for protein transport and communication within the compartments. The transfer of the genome from the gram-negative eubacterium to the newly formed nucleus and an assortment and integration of genes from the two partners led to the formation of the ancestral eukary
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Archaebacteria but instead was a chimera formed by fusion and integration of the genomes of an archaebacterium and a gram-negative bacterium. The available data indicate that the primary fusion event that gave rise to the ancestral eukaryotic cell was unique and that it was very probably distinct from (and preceded) the one that gave rise to mitochondria and hydrogenosomes. These results provide e
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Archaebacteria but instead was a chimera formed by fusion and integration of the genomes of an archaebacterium and a gram-negative bacterium. The available data indicate that the primary fusion event that gave rise to the ancestral eukaryotic cell was unique and that it was very probably distinct from (and preceded) the one that gave rise to mitochondria and hydrogenosomes. These results provide e
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family. Mol. Cell. Biol. 10:5160?5165. 3. Alberts, B., D. Bray, J. Lewis, M. Raff, K. Roberts, and J. D. Watson. 1994. Molecular biology of the cell. Garland Publishing, Inc., New York, N.Y. 4. Allsopp, A. 1969. Phylogenetic relationships of the procaryota and the origin of the e
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli
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Ell, T., and R. G. E. Murray. 1986. Polar lipid profiles of the genus Deinococcus. Int. J. Syst. Bacteriol. 36:202?06. 40. Craig, E. A. 1993. Chaperones: helpers along the pathways to protein folding. Science 260:1902?903. 41. Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402?14. 42. Creti, R., E. Ceccarelli