Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins

Summary: Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous pro...

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Autores principales:	Michael Liebthal, Manish Singh Kushwah, Philipp Kukura, Karl-Josef Dietz
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Biophysical chemistry Protein Structural biology Science Q
Acceso en línea:	https://doaj.org/article/85ded21635dd48d1b57d2eff9c497998
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spelling	oai:doaj.org-article:85ded21635dd48d1b57d2eff9c4979982021-11-20T05:08:58ZSingle molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins2589-004210.1016/j.isci.2021.103258https://doaj.org/article/85ded21635dd48d1b57d2eff9c4979982021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S258900422101227Xhttps://doaj.org/toc/2589-0042Summary: Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein complexes in solution. We demonstrate these capabilities by studying the functionally relevant oligomeric equilibria of 2-cysteine peroxiredoxins (2CPs). Comparison of the polydispersity of plant and human 2CPs as a function of concentration and redox state revealed features conserved among all 2CPs. In addition, we also find species-specific differences in oligomeric transitions, the occurrence of intermediates and the formation of high molecular weight complexes, which are associated with chaperone activity or act as a storage pool for more efficient dimers outlining the functional differentiation of human 2CPs. Our results point to a diversified functionality of oligomerization for 2CPs and illustrate the power of mass photometry for characterizing heterogeneous oligomeric protein distributions in near native conditions.Michael LiebthalManish Singh KushwahPhilipp KukuraKarl-Josef DietzElsevierarticleBiophysical chemistryProteinStructural biologyScienceQENiScience, Vol 24, Iss 11, Pp 103258- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biophysical chemistry Protein Structural biology Science Q
spellingShingle	Biophysical chemistry Protein Structural biology Science Q Michael Liebthal Manish Singh Kushwah Philipp Kukura Karl-Josef Dietz Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
description	Summary: Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein complexes in solution. We demonstrate these capabilities by studying the functionally relevant oligomeric equilibria of 2-cysteine peroxiredoxins (2CPs). Comparison of the polydispersity of plant and human 2CPs as a function of concentration and redox state revealed features conserved among all 2CPs. In addition, we also find species-specific differences in oligomeric transitions, the occurrence of intermediates and the formation of high molecular weight complexes, which are associated with chaperone activity or act as a storage pool for more efficient dimers outlining the functional differentiation of human 2CPs. Our results point to a diversified functionality of oligomerization for 2CPs and illustrate the power of mass photometry for characterizing heterogeneous oligomeric protein distributions in near native conditions.
format	article
author	Michael Liebthal Manish Singh Kushwah Philipp Kukura Karl-Josef Dietz
author_facet	Michael Liebthal Manish Singh Kushwah Philipp Kukura Karl-Josef Dietz
author_sort	Michael Liebthal
title	Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
title_short	Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
title_full	Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
title_fullStr	Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
title_full_unstemmed	Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
title_sort	single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/85ded21635dd48d1b57d2eff9c497998
work_keys_str_mv	AT michaelliebthal singlemoleculemassphotometryrevealsthedynamicoligomerizationofhumanandplantperoxiredoxins AT manishsinghkushwah singlemoleculemassphotometryrevealsthedynamicoligomerizationofhumanandplantperoxiredoxins AT philippkukura singlemoleculemassphotometryrevealsthedynamicoligomerizationofhumanandplantperoxiredoxins AT karljosefdietz singlemoleculemassphotometryrevealsthedynamicoligomerizationofhumanandplantperoxiredoxins
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Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins

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