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Paleoproteomics characterization of fossil arthropod parasitiformes amber inclusions

ABSTRACT: In this study, we developed and applied a paleoproteomics approach to study inclusions of fossil arthropod parasitiformes in two Burmese amber (Cretaceous, ca. 124 - 99 mya) pieces. The results supported the identification of Cornupalpatum sp. and the first report of fossil Holothyrida, Neothyridae at both morphological and molecular levels. Identified proteins were analyzed to evaluate evolutionary trees with possible functional implications in biomedicine. Actin proteins were identified in both amber inclusions and may belong to Neothyridae and Cornupalpatum sp., respectively.

INSTRUMENT(S):

ORGANISM(S): Holothyrida

SUBMITTER: Margarita Villar

LAB HEAD: Margarita Villar

PROVIDER: PXD055542 | Pride | 2025-11-06

REPOSITORIES: Pride

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			Action	DRS
	Control-1.wiff	Wiff
	Control-1.wiff.scan	Wiff
	Control-IXO.group	Other
	Control-Mite.group	Other
	IXO-1.wiff	Wiff

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SILAC proteomics on MG132-induced nuclear aggregates

Project description:H1299 cells were labelled either with light (Lys0/Arg0) or heavy (Lys8/Arg10) amino acids and were either unstressed (light), stressed (heavy) with MG132 (15hrs) or stressed with MG132 and allowed to recover for 8hrs (light). Equal number of unstressed and MG132 stressed cells or MG132 stressed cells and cells after 8hrs recovery were mixed before isolation of nuclear inclusions (N-Lauroylsarcosine insoluble inclusions). Isolated inclusions were solubilised in 5% SDS before trypsin digestion (10g of sample) in columns using the universal proteomics sample preparation kit ProtiFi according to manufacturer’s instructions before eluted peptides were analysed by mass-spectrometry. Quantitation of data from 3 independent experiments.

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Inclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation

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