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Anthony De Tomaso

Anthony De Tomaso

· Professor

University of California, Santa Barbara · Molecular, Cellular, and Developmental Biology

Active 2002–2024

h-index4
Citations2.0k
Papers71 last 5y
Funding$6.7M
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About

Anthony De Tomaso received his BS degree in Biology from Stanford University and his PhD in Cellular and Molecular Biology at Washington University School of Medicine in St. Louis. His doctoral thesis focused on understanding the mechanisms of multi-subunit protein assembly and targeting, using the rodent Na,K-ATPase. Following his PhD, he was an NIH fellow in the laboratory of Irv Weissman at Stanford University, where he worked on delineating the molecular mechanisms underlying allorecognition in the primitive chordate Botryllus schlosseri, as well as understanding the cellular and molecular basis of regeneration in this organism. His research is centered around the phenomenon of self/non-self recognition (allorecognition) in Botryllus schlosseri, a primitive chordate organism. This allorecognition reaction links fields such as immunology, stem cell biology, developmental biology, and evolutionary biology, with ecological implications. His lab uses genetic, genomic, and cell biological approaches to understand the molecular mechanisms behind this reaction, which is similar to MHC-based allorecognition in vertebrates and resembles bone marrow transplant recognition and rejection in mice and humans. The research also explores how transplanted stem cells parasitize other individuals, a process genetically determined and autonomous to the cells. Botryllus's colonial and asexual reproductive capabilities, which allow regeneration without embryonic stages, make it a unique model for studying developmental pathways involved in regeneration and chordate evolution. His work aims to provide insights into the origins of chordate innovations and the mechanisms underlying self/non-self recognition and regeneration.

Research topics

  • Ecology
  • Fishery
  • Physics
  • Biology

Selected publications

  • Deep quantitative proteomics of North American Pacific coast star tunicate (Botryllus schlosseri)

    Authorea (Authorea) · 2024

    • Fishery
    • Biology
    • Ecology

    Botryllus schlosseri , is a model marine invertebrate for studying immunity, regeneration, and stress-induced evolution. Conditions for validating its predicted proteome were optimized using nanoElute® 2 deep-coverage LCMS, revealing up to 4,930 protein groups and 20,984 unique peptides per sample. Spectral libraries were generated and filtered to remove interferences, low-quality transitions, and only retain proteins with >3 unique peptides. The resulting DIA assay library enabled label-free quantitation of 3,426 protein groups represented by 22,593 unique peptides. Quantitative comparisons of a laboratory-raised with two field-collected populations revealed (1) a more unique proteome in the laboratory-raised population, and (2) proteins with high/low individual variabilities in each population. DNA repair/replication, ion transport, and intracellular signaling processes were unique in laboratory-cultured colonies. Spliceosome and Wnt signaling proteins were the least variable (highly functionally constrained) in all populations. In conclusion, we present the first colonial tunicate’s deep quantitative proteome analysis, identifying functional protein clusters associated with laboratory conditions, different habitats, and strong versus relaxed abundance constraints. These results empower research on B. schlosseri with proteomics resources and enable quantitative molecular phenotyping of changes associated with transfer from in situ to ex situ and from in vivo to in vitro culture conditions.

  • Selection, drift, and constraint in cypridinid luciferases and the diversification of bioluminescent signals in sea fireflies

    Molecular Ecology · 2020 · 26 citations

    • Biology
    • Evolutionary biology
    • Genetics

    Understanding the genetic causes of evolutionary diversification is challenging because differences across species are complex, often involving many genes. However, cases where single or few genetic loci affect a trait that varies dramatically across a radiation of species provide tractable opportunities to understand the genetics of diversification. Here, we begin to explore how diversification of bioluminescent signals across species of cypridinid ostracods ("sea fireflies") was influenced by evolution of a single gene, cypridinid-luciferase. In addition to emission spectra ("colour") of bioluminescence from 21 cypridinid species, we report 13 new c-luciferase genes from de novo transcriptomes, including in vitro assays to confirm function of four of those genes. Our comparative analyses suggest some amino acid sites in c-luciferase evolved under episodic diversifying selection and may be associated with changes in both enzyme kinetics and colour, two enzymatic functions that directly impact the phenotype of bioluminescent signals. The analyses also suggest multiple other amino acid positions in c-luciferase evolved neutrally or under purifying selection, and may have impacted the variation of colour of bioluminescent signals across genera. Previous mutagenesis studies at candidate sites show epistatic interactions, which could constrain the evolution of c-luciferase function. This work provides important steps toward understanding the genetic basis of diversification of behavioural signals across multiple species, suggesting different evolutionary processes act at different times during a radiation of species. These results set the stage for additional mutagenesis studies that could explicitly link selection, drift, and constraint to the evolution of phenotypic diversification.

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