Origin of complexity in haemoglobin evolution.

ABSTRACT: Most proteins associate into multimeric complexes with specific architectures^1,2, which often have functional properties such as cooperative ligand binding or allosteric regulation³. No detailed knowledge is available about how any multimer and its functions arose during evolution. Here we use ancestral protein reconstruction and biophysical assays to elucidate the origins of vertebrate haemoglobin, a heterotetramer of paralogous α- and β-subunits that mediates respiratory oxygen transport and exchange by cooperatively binding oxygen with moderate affinity. We show that modern haemoglobin evolved from an ancient monomer and characterize the historical 'missing link' through which the modern tetramer evolved-a noncooperative homodimer with high oxygen affinity that exi

SUBMITTER: Pillai AS 

PROVIDER: S-EPMC8259614 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature