Modern and Fossil Coral Skeletal Proteomes - Fossil Insoluble Trypsin2

ABSTRACT: Here we report the first recovery, sequencing, and identification of fossil biomineral proteins from a Pleistocene invertebrate. Fossils of the Caribbean stony coral Orbicella annularis retain total hydrolyzable amino acids of a similar composition to extracts from modern O. annularis skeletons and ~10% of the modern skeletal proteome was sequenced by LC-MS/MS over multiple trials in the best-preserved fossil coral specimen. The data are rich in acidic amino acids such as aspartate and glutamate typical of skeletal proteins, and one of the four sequenced fossil proteins, a highly acidic protein, has been previously characterized in modern coral skeletons. A combination of degradation, or amino acid racemization inhibition of trypsin digestion, appears to limit greater recovery. Nevertheless, our workflow determines optimal samples for effective sequencing of fossil coral proteins, allowing comparison of modern and fossil invertebrate protein sequences, and will likely lead to further improvements of the methods. Sequencing of endogenous organic molecules in fossil biominerals provides an ancient record of composition, potentially clarifying evolutionary changes and biotic responses to paleoenvironments.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Orbicella Annularis

TISSUE(S): Skeleton

DISEASE(S): Wounds And Injuries

SUBMITTER: Jeana Drake  

LAB HEAD: David Jacobs

PROVIDER: PXD017880 | Pride | 2020-10-27

REPOSITORIES: Pride