{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,9,16]],"date-time":"2023-09-16T05:40:21Z","timestamp":1694842821143},"reference-count":46,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2014,4,5]],"date-time":"2014-04-05T00:00:00Z","timestamp":1396656000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"NIH","award":["PN2EY016525, R01EY015834"],"award-info":[{"award-number":["PN2EY016525, R01EY015834"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2014,6]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The features in partially folded intermediates that allow the group II chaperonins to distinguish partially folded from native states remain unclear. The archaeal group II chaperonin from <jats:italic>Methanococcus Mauripaludis<\/jats:italic> (Mm\u2010Cpn) assists the <jats:italic>in vitro<\/jats:italic> refolding of the well\u2010characterized \u03b2\u2010sheet lens protein human \u03b3D\u2010crystallin (H\u03b3D\u2010Crys). The domain interface and buried cores of this Greek key conformation include side chains, which might be exposed in partially folded intermediates. We sought to assess whether particular features buried in the native state, but absent from the native protein surface, might serve as recognition signals. The features tested were (a) paired aromatic side chains, (b) side chains in the interface between the duplicated domains of H\u03b3D\u2010Crys, and (c) side chains in the buried core which result in congenital cataract when substituted. We tested the Mm\u2010Cpn suppression of aggregation of these H\u03b3D\u2010Crys mutants upon dilution out of denaturant. Mm\u2010Cpn was capable of suppressing the off\u2010pathway aggregation of the three classes of mutants indicating that the buried residues were not recognition signals. In fact, Mm\u2010Cpn recognized the H\u03b3D\u2010Crys mutants better than (wild\u2010type) WT and refolded most mutant H\u03b3D\u2010Crys to levels twice that of WT H\u03b3D\u2010Crys. This presumably represents the increased population or longer lifetimes of the partially folded intermediates of the mutant proteins. The results suggest that Mm\u2010Cpn does not recognize the features of H\u03b3D\u2010Crys tested\u2014paired aromatics, exposed domain interface, or destabilized core\u2014but rather recognizes other features of the partially folded \u03b2\u2010sheet conformation that are absent or inaccessible in the native state of H\u03b3D\u2010Crys.<\/jats:p>","DOI":"10.1002\/pro.2452","type":"journal-article","created":{"date-parts":[[2014,3,10]],"date-time":"2014-03-10T09:30:45Z","timestamp":1394443845000},"page":"693-702","source":"Crossref","is-referenced-by-count":2,"title":["Group II archaeal chaperonin recognition of partially folded human \u03b3D\u2010crystallin mutants"],"prefix":"10.1002","volume":"23","author":[{"given":"Oksana A.","family":"Sergeeva","sequence":"first","affiliation":[{"name":"Department of Biology Massachusetts Institute of Technology Cambridge Massachusetts 02139"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jingkun","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Biology Massachusetts Institute of Technology Cambridge Massachusetts 02139"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan A.","family":"King","sequence":"additional","affiliation":[{"name":"Department of Biology Massachusetts Institute of Technology Cambridge Massachusetts 02139"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kelly M.","family":"Knee","sequence":"additional","affiliation":[{"name":"Rare Disease Research Unit, Pfizer Inc. 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