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Dilution of the [GroEL\u2010substrate protein] binary complex prior to ATP addition significantly improved the yield of folding, suggesting that the released protein has a tendency to aggregate. When <jats:italic>N<\/jats:italic>\u2010ethylmaleimide treated GroEL, which can form the binary complex but not release the bound protein, was added to the binary complex prior to ATP addition, productive folding was severely inhibited, indicating that the protein released from GroEL\/ES can bind to <jats:italic>N<\/jats:italic>\u2010ethylmaleimide treated chaperonin. These data favor the \u2018reservoir\u2019 or \u2018reversion\u2019 model, in which GroEL\/ES acts as a buffer of folding intermediate or mediates reversion of a misfolded protein to a less folded primitive form, rather than the \u2018marsupium\u2019 model in which folding of the substrate protein proceeds in chaperonin.<\/jats:p>","DOI":"10.1016\/0014-5793(95)00041-7","type":"journal-article","created":{"date-parts":[[2003,4,25]],"date-time":"2003-04-25T01:18:33Z","timestamp":1051233513000},"page":"195-198","source":"Crossref","is-referenced-by-count":32,"title":["Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin"],"prefix":"10.1002","volume":"359","author":[{"given":"Hideki","family":"Taguchi","sequence":"first","affiliation":[]},{"given":"Masasuke","family":"Yoshida","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2000,2,23]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/333330a0"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.60.070191.001541"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/355033a0"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1993.0030"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.cb.09.110193.003125"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(93)90470-B"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(79)90502-3"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(79)90501-1"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(92)80240-H"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/371578a0"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(93)80838-L"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)37227-7"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.62.070193.002025"},{"key":"e_1_2_1_15_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pp.45.060194.002345"},{"key":"e_1_2_1_16_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bb.23.060194.003241"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00220a020"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1993.0029"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560010711"},{"key":"e_1_2_1_20_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.7913555"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1038\/366228a0"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.8100365"},{"key":"e_1_2_1_23_1","unstructured":"B. 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