NDLI: Disulfide formation as a probe of folding in GroEL–GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones

Content Provider	PubMed Central
Author	Park, Eun Sun Fenton, Wayne A. Horwich, Arthur L.
Copyright Year	2007
Abstract	The chaperonin GroEL assists protein folding by binding nonnative forms through exposed hydrophobic surfaces in an open ring and mediating productive folding in an encapsulated hydrophilic chamber formed when it binds GroES. Little is known about the topology of nonnative proteins during folding inside the GroEL–GroES cis chamber. Here, we have monitored topology employing disulfide bond formation of a secretory protein, trypsinogen (TG), that behaves in vitro as a stringent, GroEL–GroES-requiring substrate. Inside the long-lived cis chamber formed by SR1, a single-ring version of GroEL, complexed with GroES, we observed an ordered formation of disulfide bonds. First, short-range disulfides relative to the primary structure formed, both native and nonnative. Next, the two long-range native disulfides that “pin” the two β-barrel domains together formed. Notably, no long-range nonnative bonds were ever observed, suggesting that a native-like long-range topology is favored. At both this time and later, however, the formation of several medium-range nonnative bonds mapping to one of the β-barrels was observed, reflecting that the population of local nonnative structure can occur even within the cis cavity. Yet both these and the short-range nonnative bonds were ultimately “edited” to native, as evidenced by the nearly complete recovery of native TG. We conclude that folding in the GroEL–GroES cavity can favor the formation of a native-like topology, here involving the proper apposition of the two domains of TG; but it also involves an ATP-independent conformational “editing” of locally incorrect structures produced during the dwell time in the cis cavity.
Related Links	http://dx.doi.org/10.1073/pnas.0610989104
Ending Page	2150
Page Count	6
Starting Page	2145
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	104
Language	English
Publisher	National Academy of Sciences
Publisher Date	2007-02-13
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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