Origin of complexity in hemoglobin evolution

@article{Pillai2020OriginOC,
  title={Origin of complexity in hemoglobin evolution},
  author={Arvind S. Pillai and Shane A. Chandler and Yang Liu and Anthony V. Signore and Carlos R. Cortez-Romero and Justin L. P. Benesch and Arthur Laganowsky and Jay F. Storz and Georg K. A. Hochberg and Joseph W. Thornton},
  journal={Nature},
  year={2020},
  volume={581},
  pages={480 - 485}
}
Most proteins associate into multimeric complexes with specific architectures 1 , 2 , which often have functional properties such as cooperative ligand binding or allosteric regulation 3 . 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… 
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References

SHOWING 1-10 OF 85 REFERENCES
Hemoglobin function in the vertebrates: An evolutionary model
  • M. Coates
  • Biology
    Journal of Molecular Evolution
  • 2005
TLDR
It is proposed that from the monomeric hemoglobin of the common ancestor of vertebrates, a deoxy dimer could have originated with a single amino acid substitution, as seen in the lamprey, and has a Bohr effect, cooperativity and a reduced oxygen affinity compared to the monomers.
Evolution of increased complexity in a molecular machine
TLDR
It is shown that the ring of Fungi, which is composed of three paralogous proteins, evolved from a more ancient two-paralogue complex because of a gene duplication that was followed by loss in each daughter copy of specific interfaces by which it interacts with other ring proteins.
Anionic Control of Function in Vertebrate Hemoglobins
Point mutations in the amino acid sequence of normal human hemoglobin have provided a powerful means of probing structure-function relationships in this respiratory protein. Through studies of
Evolutionary diversification of the multimeric states of proteins
  • M. Lynch
  • Biology
    Proceedings of the National Academy of Sciences
  • 2013
TLDR
It is suggested that variation in the multimeric states of proteins can readily arise from stochastic transitions resulting from the joint processes of mutation and random genetic drift, even in the face of constant directional selection for one particular protein architecture across all lineages.
Proteins evolve on the edge of supramolecular self-assembly
TLDR
Point mutations can frequently trigger folded proteins to self-assemble into higher-order structures and this potential is counterbalanced by negative selection and can be exploited to design nanomaterials in living cells.
Structure, dynamics, assembly, and evolution of protein complexes.
TLDR
Major advances have been made in the understanding of protein complex evolution, both in reconstructing evolutionary histories of specific complexes and in elucidating general mechanisms that explain how quaternary structure tends to evolve.
...
...