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Using\n                    <jats:italic>Chlamydomonas reinhardtii<\/jats:italic>\n                    as a model system, we found that\n                    <jats:italic>in\u00a0vivo<\/jats:italic>\n                    the chloroplast chaperonin consists of CPN60\u03b1, CPN60\u03b21 and CPN60\u03b22 and the co\u2010chaperonin of the three subunits CPN20, CPN11 and CPN23. In\n                    <jats:italic>Escherichia coli,<\/jats:italic>\n                    CPN20 homo\u2010oligomers and all possible other chloroplast co\u2010chaperonin hetero\u2010oligomers are functional, but only that consisting of CPN11\/20\/23\u2010CPN60\u03b1\u03b21\u03b22 can fully replace GroES\/GroEL under stringent stress conditions. Endogenous CPN60 was purified and its stoichiometry was determined to be 6:2:6 for CPN60\u03b1:CPN60\u03b21:CPN60\u03b22. The cryo\u2010EM structures of endogenous CPN60\u03b1\u03b21\u03b22\/ADP and CPN60\u03b1\u03b21\u03b22\/co\u2010chaperonin\/ADP were solved at resolutions of 4.06 and 3.82\u00a0\u00c5, respectively. In both hetero\u2010oligomeric complexes the chaperonin subunits within each ring are highly symmetric. Through hetero\u2010oligomerization, the chloroplast co\u2010chaperonin CPN11\/20\/23 forms seven GroES\u2010like domains, which symmetrically interact with CPN60\u03b1\u03b21\u03b22. Our structure also reveals an uneven distribution of roof\u2010forming domains in the dome\u2010shaped CPN11\/20\/23 co\u2010chaperonin and potentially diversified surface properties in the folding cavity of the CPN60\u03b1\u03b21\u03b22 chaperonin that might enable the chloroplast chaperonin system to assist in the folding of specific substrates.\n                  <\/jats:p>","DOI":"10.1111\/tpj.14273","type":"journal-article","created":{"date-parts":[[2019,2,8]],"date-time":"2019-02-08T12:07:33Z","timestamp":1549627653000},"page":"798-812","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Hetero\u2010oligomeric CPN60 resembles highly symmetric group\u2010I chaperonin structure revealed by Cryo\u2010EM"],"prefix":"10.1111","volume":"98","author":[{"given":"Qian","family":"Zhao","sequence":"first","affiliation":[{"name":"State Key Laboratory of Plant Cell and Chromosome Engineering Institute of Genetics and Developmental Biology The Innovative Academy of Seed Design Chinese Academy of Sciences Beijing 100101 China"},{"name":"University of Chinese Academy of Sciences Beijing 100101 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang","family":"Zhang","sequence":"additional","affiliation":[{"name":"National Center for Protein Science Shanghai State Key Laboratory of Molecular Biology CAS Center for Excellence in Molecular Cell Science Shanghai Institute of Biochemistry and Cell Biology Chinese Academy of Sciences University of Chinese Academy of Sciences Shanghai 201210 China"},{"name":"Shanghai Science Research Center Chinese Academy of Sciences Shanghai 201210 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frederik","family":"Sommer","sequence":"additional","affiliation":[{"name":"Shanghai Science Research Center Chinese Academy of Sciences Shanghai 201210 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