16 research outputs found
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Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry.
Small heat shock proteins (sHSP) are a remarkably diverse group of molecular chaperones possessing a degree of structural plasticity unparalleled in other protein superfamilies. In the absence of chemical energy input, these stability sensors can sensitively recognize and bind destabilized proteins, even in the absence of gross misfolding. Cellular conditions regulate affinity towards client proteins allowing tightly controlled switching and tuning of sHSP chaperone capacity. Perturbations of this regulation, through chemical modification or mutation, directly lead to a variety of diseased states. This review explores the structural basis of sHSP oligomeric flexibility and the corresponding functional consequences in the context of a model describing sHSP activity with a set of three coupled thermodynamic equilibria. As current research illuminates many novel physiological roles for sHSP outside of their traditional duties as molecular chaperones, such a conceptual framework provides a sound foundation to describe these emerging functions in physiological and pathological processes
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Shotgun and TMT-Labeled Proteomic Analysis of the Ovarian Proteins of an Insect Vector, Aedes aegypti (Diptera: Culicidae)
Aedes aegypti [Linnaeus in Hasselquist; yellow fever mosquito] transmits several viruses that infect millions of people each year, including Zika, dengue, yellow fever, chikungunya, and West Nile. Pathogen transmission occurs during blood feeding. Only the females blood feed as they require a bloodmeal for oogenesis; in the bloodmeal, holo-transferrin and hemoglobin provide the females with a high iron load. We are interested in the effects of the bloodmeal on the expression of iron-associated proteins in oogenesis. Previous data showed that following digestion of a bloodmeal, ovarian iron concentrations doubles by 72 hr. We have used shotgun proteomics to identify proteins expressed in Ae. aegypti ovaries at two oogenesis developmental stages following blood feeding, and tandem mass tag-labeling proteomics to quantify proteins expressed at one stage following feeding of a controlled iron diet. Our findings provide the first report of mosquito ovarian protein expression in early and late oogenesis. We identify proteins differentially expressed in the two oogenesis development stages. We establish that metal-associated proteins play an important role in Ae. aegypti oogenesis and we identify new candidate proteins that might be involved in mosquito iron metabolism. Finally, this work identified a unique second ferritin light chain subunit, the first reported in any species. The shotgun proteomic data are available via ProteomeXchange with identifier PXD005893, while the tandem mass tag-labeled proteomic data are available with identifier PXD028242. © The Author(s) 2022. Published by Oxford University Press on behalf of Entomological Society of America.Open access journalThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at [email protected]