Dataset Information

Thermal proteome profiling of sponge whole-body movement

ABSTRACT: Sponges (Porifera) are early-branching Metazoa who do not possess muscles or neurons, however are able to undergo a whole-body movement that involves the closure of their canal system and collapse of an epithelial tent. In this study we profile proteomic responses of the freshwater sponge Spongilla lacustris during nitric oxide (NO) and agitation induced movements to elucidate the early evolution of coordination. Specifically, we measure condition-dependent changes in protein thermal stability and abundance using Thermal proteome profiling (TPP). These changes are the result of proteins undergoing stabilizing or destabilizing conformational changes broadly caused by e.g. the binding or dissociation of small molecules to the proteins, the formation or loss of protein-protein interactions or a change in post-translational modifications.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Spongilla Lacustris

TISSUE(S): Whole Body

SUBMITTER: Frank Stein

LAB HEAD: Detlev Arendt

PROVIDER: PXD044169 | Pride | 2024-01-04

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Ernie_S1799_IB_FR_sponges2DTPP_T1T2_R1_F1.raw	Raw
	Ernie_S1799_IB_FR_sponges2DTPP_T1T2_R1_F10.raw	Raw
	Ernie_S1799_IB_FR_sponges2DTPP_T1T2_R1_F11.raw	Raw
	Ernie_S1799_IB_FR_sponges2DTPP_T1T2_R1_F12.raw	Raw
	Ernie_S1799_IB_FR_sponges2DTPP_T1T2_R1_F2.raw	Raw

Items per page:

1 - 5 of 120

Similar Datasets

Project description:Organisms across all kingdoms of life use small organic molecules called osmolytes to adapt to diverse environmental conditions and preserve viability. Osmolytes are thought to thermally stabilise proteins based on in vitro studies of a few purified proteins. The molecular mechanisms of osmolytes remain controversial and systematic global studies of osmolyte action within a complex cellular milieu are so far lacking. Here we present an in situ proteome-wide analysis of protein thermal stabilisation by osmolytes, covering all major classes of these molecules: trimethylamine N-oxide (TMAO), betaine, glycerol, proline, trehalose and glucose. Using a structural proteomics approach, we systematically probed the effects of osmolytes on protein thermal stability, native structures, and aggregation, thus revealing widespread mechanisms of osmolyte action, but also osmolyte- and protein- specific effects. All tested osmolytes stabilised the majority of the proteome. The stabilisation of most proteins could be explained by the preferential exclusion model, according to which osmolytes unfavourably interact with protein backbones thus promoting folded states. We also detected specific protein-osmolyte binding events which resulted in strong thermal stabilisation, although binding was not necessary for stabilisation. Aggregation of most proteins occurred at higher temperatures in the presence of osmolytes than in their absence. TMAO however promoted aggregation of small, unfolded proteins but also showed the strongest protein thermal stabilisation effects, which might reflect adaptation to the extreme living conditions of marine organisms that accumulate TMAO. Our global in situ analysis provides mechanistic insight into how osmolytes function within a complex biological matrix. Our data further provides a resource to guide the design or selection of stabilisers for protein-based drugs and the identification of conditions that increase thermotolerance of microorganisms in biotechnological applications.

Dataset Information

Thermal proteome profiling of sponge whole-body movement

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets