Project description:Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functional evolution. For instance, we show that TERF1 evolved as a telomere-binding protein in the common stem lineage of marsupial and placental mammals. Phylointeractomics is a versatile and scalable approach to investigate evolutionary changes in protein function and thus can provide experimental evidence for phylogenomic relationships.
Project description:We report the transcriptional response to Colorado potato beetle herbivory in leaves of the highly beetle resistant Solanum chacoense diploid line USDA8380-1 (80-) and a susceptible F2 individual (EE501F2_093) derived from a cross between 80-1 and a beetle susceptible line S. chacoense M6. Sampling tissue in a time course during adult Colorado potato beetle feeding provides novel insight to the transcriptomic defense response to this important pest.
Project description:16S amplicon pool analyses of the four gut sections of the wood-feeding beetle, Odontotaenius disjunctus The beetle is purely wood feeding, and we aim to first characterize the community that exist within the gut sections 4 beetles, four gut sections per beetle, one PhyloChip per gut section, total = 16 chips
Project description:How novel genes and cellular functions evolve is a central question in biology. Exon shuffling represents a potent mechanism to assemble new protein architectures. Here we show that DNA transposons, which are mobile and pervasive in genomes, have provided a recurrent supply of both exons and splice sites to assemble novel protein-coding genes in vertebrates. We find that transposase domains have been captured, primarily via alternative splicing, to form new fusion proteins at least 99 times independently over ~350 million years of tetrapod evolution. Evolution favors fusion of transposase DNA-binding domains to host regulatory domains, especially the Krüppel-associated Box (KRAB), suggesting transposase capture frequently yields new transcriptional repressors. Consistent with this model, we show that four KRAB-transposase fusion proteins born independently in different mammalian lineages repress gene expression in a sequence-specific fashion. Genetic knockout and rescue of the bat-specific KRABINER fusion protein in cell culture demonstrates that it binds its cognate transposons genome wide and controls a network of genes and cis-regulatory elements. Transposase capture is thus a powerful mechanism whereby transcription factors and their associated cis-regulatory networks can evolve by repurposing DNA transposon families, which provide both DNA binding domains and pre-existing genomic binding sites.