Molecular chaperon produced by an intracellular symbiont.
Symbionin, that is selectively produced by an intracellular symbiont harbored by the aphid bacteriocyte, is structurally homologous to the Escherichia coli groEL protein, a heat shock protein functioning as a molecular chaperon. It was shown that symbionin has ATPase activity and, in the presence of Mg-ATP, is converted into lower molecular mass species. Like the groEL protein, symbionin was able to reconstitute dimeric ribulose 1,5-bisphosphate carboxylase/oxygenase holoenzyme from its unfolded subunits in vitro, suggesting that this protein functions as a molecular chaperon in the endosymbiont. The groES-homologous protein did exist in the endosymbiont, but its amount was small relative to that of symbionin.
Zoological Institute, Faculty of Science, University of Tokyo.
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Kakeda
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Ishikawa
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001042:Aphids / Q000382:microbiology*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000378:metabolism; D018834:Chaperonin 60; D018833:Chaperonins; D004926:Escherichia coli / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D007301:Insect Hormones / Q000096:biosynthesis*; D046911:Macromolecular Substances; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D013559:Symbiosis
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D007301:Insect Hormones; D046911:Macromolecular Substances; D011506:Proteins; C044322:SymL protein, Bacteria; D000251:Adenosine Triphosphatases; D018833:Chaperonins; D012273:Ribulose-Bisphosphate Carboxylase