Conformational folding and disulfide bonding drive distinct stages of protein structure formation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Jian-Min Lv, Shou-Qin Lü, Zu-Pei Liu, Juan Zhang, Bo-Xuan Gao, Zhen-Yu Yao, Yue-Xin Wu, Lawrence A. Potempa, Shang-Rong Ji, Mian Long, Yi Wu

ABSTRACT

The causal relationship between conformational folding and disulfide bonding in protein oxidative folding remains incompletely defined. Here we show a stage-dependent interplay between the two events in oxidative folding of C-reactive protein (CRP) in live cells. CRP is composed of five identical subunits, which first fold spontaneously to a near-native core with a correctly positioned C-terminal helix. This process drives the formation of the intra-subunit disulfide bond between Cys36 and Cys97. The second stage of subunit folding, however, is a non-spontaneous process with extensive restructuring driven instead by the intra-subunit disulfide bond and guided by calcium binding-mediated anchoring. With the folded subunits, pentamer assembly ensues. Our results argue that folding spontaneity is the major determinant that dictates which event acts as the driver. The stepwise folding pathway of CRP further suggests that one major route might be selected out of the many in theory for efficient folding in the cellular environment. More... »

PAGES

1494

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-20014-y

DOI

http://dx.doi.org/10.1038/s41598-018-20014-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1100512294

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29367639


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39 schema:description The causal relationship between conformational folding and disulfide bonding in protein oxidative folding remains incompletely defined. Here we show a stage-dependent interplay between the two events in oxidative folding of C-reactive protein (CRP) in live cells. CRP is composed of five identical subunits, which first fold spontaneously to a near-native core with a correctly positioned C-terminal helix. This process drives the formation of the intra-subunit disulfide bond between Cys36 and Cys97. The second stage of subunit folding, however, is a non-spontaneous process with extensive restructuring driven instead by the intra-subunit disulfide bond and guided by calcium binding-mediated anchoring. With the folded subunits, pentamer assembly ensues. Our results argue that folding spontaneity is the major determinant that dictates which event acts as the driver. The stepwise folding pathway of CRP further suggests that one major route might be selected out of the many in theory for efficient folding in the cellular environment.
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