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Related Concept Videos

Gene Duplication and Divergence02:37

Gene Duplication and Divergence

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The seminal work of Ohno in 1970 popularized the idea of gene duplication and divergence. DNA sequence comparison studies reveal that a large portion of the genes in bacteria, archaebacteria, and eukaryotes was  generated by gene duplication and divergence, indicating its critical role in evolution.
The duplicated copies of the gene are called Paralogs. Paralogs with similar sequences and functions form a gene family. Across several species, a large number of gene families are...
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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Measurement of Heme Synthesis Levels in Mammalian Cells
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Origin of complexity in haemoglobin evolution.

Arvind S Pillai1, Shane A Chandler2, Yang Liu3

  • 1Department of Ecology and Evolution, University of Chicago, Chicago, IL, USA.

Nature
|May 29, 2020
PubMed
Summary
This summary is machine-generated.

Modern hemoglobin evolved from an ancient single-unit protein. Researchers traced its evolutionary path through a dimeric intermediate, revealing how gene duplication and key mutations created its complex structure and cooperative oxygen binding.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Biochemistry

Background:

  • Proteins form complex structures (multimers) with specialized functions like cooperative ligand binding.
  • The evolutionary origins of these complex protein structures and functions remain largely unknown.
  • Vertebrate hemoglobin, a tetramer, transports oxygen via cooperative binding.

Purpose of the Study:

  • To elucidate the evolutionary origins of vertebrate hemoglobin.
  • To identify the ancestral protein structures and evolutionary intermediates.
  • To understand the genetic and biophysical mechanisms driving the evolution of complex protein functions.

Main Methods:

  • Ancestral protein reconstruction
  • Biophysical assays
  • Comparative genomics

Main Results:

  • Modern hemoglobin evolved from an ancient monomer.
  • A noncooperative homodimer with high oxygen affinity was identified as a key evolutionary intermediate.
  • Two specific mutations were sufficient to induce tetramerization and cooperative oxygen binding in the ancestral protein.
  • An intrinsic linkage between oxygen binding and multimerization interfaces was present in the ancestral structure.

Conclusions:

  • Complex protein structures and functions can evolve through simple genetic changes.
  • Evolution can repurpose existing biophysical features to create higher-level molecular architectures.
  • The evolution of hemoglobin demonstrates a stepwise process from monomer to functional tetramer.