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FEBS Lett. 2015 Feb 13;589(4):497-499. doi: 10.1016/j.febslet.2015.01.008. Epub 2015 Jan 17.

Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system.

Author information

1
College of Pharmacy, Department of Pharmacology and Toxicology, University of Arizona, Tucson, AZ 85721.
2
Department of Genetics, Yale University School of Medicine, New Haven, CT 06510.
3
Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510.
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Contributed equally

Abstract

A recent hydrogen-deuterium exchange study of folding of the GroEL/GroES-dependent bacterial enzyme DapA has suggested that the DapA folding pathway when free in solution may differ from the folding pathway used in the presence of the GroEL/GroES chaperonin. Here, we have investigated whether DapA aggregation might be occurring in free solution under the conditions of the exchange experiment, as this would confound interpretation of the pathway predictions. Dynamic light scattering (DLS) data, sedimentation analysis and refolding yield indicate that significant aggregation occurs upon dilution of DapA from denaturant, bringing into question the earlier conclusion that different folding pathways occur in the absence and presence of the chaperonin system.

KEYWORDS:

Aggregation; DapA; GroEL; Light scattering; Protein folding

PMID:
25601566
PMCID:
PMC4410871
DOI:
10.1016/j.febslet.2015.01.008
[Indexed for MEDLINE]
Free PMC Article

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