Origin of complexity in hemoglobin evolution

  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},
  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… 

Conservation of function with diversification of higher-order structure within sensor histidine kinases

Three LOV-HK homologs are dimers with differing structural responses to light, while two are Per-ARNT-Sim (PAS)-HKs that interconvert between differentially-active monomers and dimers, suggesting dimerization as a regulatory control.

Evolutionary History of the Globin Gene Family in Annelids

The findings indicate that multiple gene duplication and neo-functionalization events shaped the evolutionary history of the globin family and report two new globin types in annelids, namely androglobins and cytoglobins.

Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.

The coupled binding and folding mechanism is overall similar, but with a higher degree of native hydrophobic contact formation in the transition state of the ancestral complex and more heterogeneous transient interactions, including electrostatic pairings, and an increased disorder for the human complex.

Evolution of the cytochrome-bd type oxygen reductase superfamily and the function of cydAA’ in Archaea

CydAA’ is the first isoform of cytbd containing only b-type hemes shown to be active when isolated, demonstrating that oxygen reductase activity in this superfamily is not dependent on heme d.

Evolution of the folding landscape of effector caspases

From hemoglobin allostery to hemoglobin-based oxygen carriers.

Joint effects of genes underlying a temperature specialization tradeoff in yeast

The joint effect of eight genes underlying thermotolerance in Saccharomyces cerevisiae, when introduced into a thermosensitive species, reveals no sign of epistasis, and suggests a principle for the field in which repacking a given protein is the hard part of evolution, and assembling combinations of unlinked loci is far easier.

Atomic-Level View of the Functional Transition in Vertebrate Hemoglobins: The Case of Antarctic Fish Hbs

The ability of MD simulations to accurately describe the functional pathway in tetrameric Hbs suggests that this approach may be effectively applied to unravel the molecular and structural basis of Hbs exhibiting peculiar functional properties as a consequence of the environmental adaptation of the host organism.

Comparative Analysis and Ancestral Sequence Reconstruction of Bacterial Sortase Family Proteins Generates Functional Ancestral Mutants with Different Sequence Specificities

It is argued that bioinformatics tools, principal component analysis and ancestral sequence reconstruction, in combination with protein biochemistry, may be used to discover or design sortases with increased catalytic efficiency and/or selectivity for sortase-mediated ligation experiments.



Hemoglobin function in the vertebrates: An evolutionary model

  • M. Coates
  • Biology
    Journal of Molecular Evolution
  • 2005
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

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
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

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.

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.