Phylointeractomics reconstructs functional evolution of protein binding

TY - JOUR

T1 - Phylointeractomics reconstructs functional evolution of protein binding

AU - Kappei, Dennis

AU - Scheibe, Marion

AU - Paszkowski-Rogacz, Maciej

AU - Bluhm, Alina

AU - Gossmann, Toni Ingolf

AU - Dietz, Sabrina

AU - Dejung, Mario

AU - Herlyn, Holger

AU - Buchholz, Frank

AU - Mann, Matthias

AU - Butter, Falk

PY - 2017/2/8

Y1 - 2017/2/8

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1038/ncomms14334

DO - 10.1038/ncomms14334

M3 - Journal article

C2 - 28176777

SN - 2041-1723

VL - 8

SP - 14334

JO - Nature Communications

JF - Nature Communications

ER -