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Tribolium castaneum

ABSTRACT: The genes responsible for avoiding attack of a beetle, relating to the duration of death feigning

PROVIDER: PRJDB11524 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	DRR286992_1.fastq.gz	Fastqsanger.gz
	DRR286992_2.fastq.gz	Fastqsanger.gz
	DRR286993_1.fastq.gz	Fastqsanger.gz
	DRR286993_2.fastq.gz	Fastqsanger.gz
	DRR286994_1.fastq.gz	Fastqsanger.gz

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Project description:The presence of DNA methylation in beetles (Coleoptera) has only been investigated with bisulfite sequencing of Tribolium castaneum, which produced no evidence of DNA methylation. Here, we used whole genome bisulfite sequencing to assay if DNA methylation was present in another beetle, Nicrophorus vespilloides. We used T. castaneum as a negative control.

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Quantitative proteomics analysis of affinity-puQuantitative proteomics analysis of affinity-purified Tribolium castaneum JHR complexesrified Tribolium castaneum JHR complexes

Project description:Juvenile hormone (JH) serves vital roles in insect reproduction, development, and many aspects of physiology. JH primarily acts at the gene-regulatory level through an intracellular receptor. The JH receptor (JHR) is a ligand-activated complex of transcription factors of the bHLH-PAS family, consisting of the JH-binding protein Methoprene-tolerant (MET) and its partner Taiman (TAI). Initial studies have indicated significance of post-transcriptional modification (phosphorylation), subunit assembly, and nucleocytoplasmic transport of JHR in JH signaling. However, our knowledge of JHR regulation at the protein level remains rudimentary, partly due to the difficulty of obtaining functional JHR proteins in a purified form. Here we present successful fermentation-level purification of JHR complexes of MET and TAI proteins from two insect species, the beetle Tribolium castaneum and the mosquito Aedes aegypti. The recombinant JHR subunits from each species were co-expressed using a baculovirus system in an insect cell line and purified through affinity steps, yielding soluble proteins, capable of binding both the hormonal ligand (JH III) and DNA bearing cognate JH-response elements. The present quantitative phosphoproteomcis analysis uncovered multiple phosphorylation sites in the TcMET protein, some of which were induced by methoprene. A functional bipartite nuclear localization signal, straddled by phosphorylated residues, was found within the disordered C-terminal region of TcMET. Our present characterization of the recombinant JHR is a primary step towards understanding JHR regulation.

2022-02-16 | PXD028599 | Pride

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