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Caracara

ABSTRACT: Ancient DNA from a 2,500-year-old Caribbean fossil places an extinct bird (Caracara creightoni) in a phylogenetic context

PROVIDER: PRJNA555901 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR9849390_1.fastq.gz	Fastqsanger.gz
	SRR9849390_2.fastq.gz	Fastqsanger.gz
	SRR9849388_1.fastq.gz	Fastqsanger.gz
	SRR9849388_2.fastq.gz	Fastqsanger.gz
	SRR9849389_1.fastq.gz	Fastqsanger.gz

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Early Pleistocene enamel proteome sequences from Dmanisi resolve Stephanorhinus phylogeny

Project description:Ancient DNA (aDNA) sequencing has enabled reconstruction of speciation, migration, and admixture events for extinct taxa. Outside the permafrost, however, irreversible aDNA post-mortem degradation has so far limited aDNA recovery to the past ~0.5 million years (Ma). Contrarily, multiple analyses suggested the presence of protein residues in Cretaceous fossil remains. Similarly, tandem mass spectrometry (MS) allowed sequencing ~1.5 million year (Ma) old collagen type I (COL1), though with limited phylogenetic use. In the absence of molecular evidence, the speciation of several Early and Middle Pleistocene extinct species remain contentious. In this study, we address the phylogenetic relationships of the Eurasian Pleistocene Rhinocerotidae using a ~1.77 Ma old dental enamel proteome of a Stephanorhinus specimen from the Dmanisi archaeological site in Georgia (South Caucasus). Molecular phylogenetic analyses place the Dmanisi Stephanorhinus as a sister group to the woolly (Coelodonta antiquitatis) and Merck’s rhinoceros (S. kirchbergensis) clade. We show that Coelodonta evolved from an early Stephanorhinus lineage and that the latter includes at least two distinct evolutionary lines. As such, the genus Stephanorhinus is currently paraphyletic and requires systematic revision. We demonstrate that Early Pleistocene dental enamel proteome sequencing overcomes the limits of ancient collagen- and aDNA-based phylogenetic inference. It also provides additional information about the sex and taxonomic assignment of the specimens analysed. Dental enamel, the hardest tissue in vertebrates, is highly abundant in the fossil record. Our findings reveal that palaeoproteomic investigation of this material can push biomolecular investigation further back into the Early Pleistocene.

2019-09-11 | PXD011008 | Pride

Project description:Molecular exploration of fossil eggshell uncovers hidden lineage of giant extinct bird

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Characterisation of eggshell proteomes from the extinct Madagascar elephant bird

Project description:Characterisation of eggshell proteomes from the extinct Madagascar elephant bird

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29 million years of diverse mammalian proteomes recovered from the East African Rift System

Project description:Here, we sample small proteomes from the interior enamel of 10 fossils deposited at seven paleontological sites between 1.5 and 29 Ma in the Turkana Basin, a region of northern Kenya in the East African Rift System. We find enamel protein fragments in all fossil specimens including a 29 Ma Arsinoitherium from Topernawi, belonging to a now extinct mammalian order. Identified proteins include the classical structural enamel proteins amelogenin, enamelin, and ameloblastin, but also uncommon enamel proteins including collagens and proteases. Protein fragment abundance and average length decline in progressively older fossils, but we observe significant variability in Early Miocene preservation from site to site, with proboscidean fossils from 16 Ma Buluk preserving substantially more proteins than Rhinocerotidae and Anthracotheriidae fossils from the marginally older Locherangan (18 Ma) and Hippopotamidae from the younger site of Napudet (c. 5-11 Ma). Most specimens yield known clade-specific diagenetiforms that support field taxonomic identifications, with the notable exception of the Arsinoitherium that is without living relatives. Consensus phylogenetic trees suggest the potential for paleoproteomics in supporting taxonomic identifications and resolving evolutionary relationships of extinct taxa but should be approached with caution due to sometimes sparse fragment identification and the potential for sequence diagenesis. We identify numerous likely modifications that support the ancient age of these proteins, and the oldest examples of advanced glycation end-products and carbamylation yet known. The persistence of protein sequences within dense enamel tissues in one of the persistently warmest places on Earth promises the discovery of far older proteomes that will aid in the study of the biology and evolutionary relationships of extinct taxa.

2023-05-02 | MSV000091838 | MassIVE

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