Correlation of DNA exonic regions with protein structural units in haemoglobin

  title={Correlation of DNA exonic regions with protein structural units in haemoglobin},
  author={Mitiko Go},
  • M. Go
  • Published 7 May 1981
  • Biology
  • Nature
The discovery of intervening sequences (introns) in DNA led Gilbert and Tonegawa1,2 to suggest that a new protein could have been produced by bringing together certain segments of pre-existing ones. However, Blake3 argued that if DNA was so organized that coding sequences (exons) correspond to structural as well as functional units of proteins, then combinations would be much more likely to yield a stable globular conformation through being ‘sums of parts’. In immunoglobulin heavy chain, four… 

Evolutionary history of introns in a multidomain globin gene

The pattern of introns in theArtemia globin gene supports a concept of general positional stability but the exceptions, where introns have moved out of reading frame, or have moved by several codons, or has been deleted, suggest that intron displacements can occur after inheritance from an ancient source.

Ancient and Recent Intron Stability in the Artemia Hemoglobin Gene

The results suggest that constraints of pre-mRNA processing should be considered when considering intron positional changes in homologous genes and the discordance of Artemia hemoglobin introns is discussed in terms of different model mechanisms and constraints.

Protein structures and split genes.

  • M. Go
  • Biology
    Advances in biophysics
  • 1985

An experimental approach to exon shuffling: Modular mutagenesis of barnase

The tertiary structure of barnase was decomposed into six modules (M1-M6) by compactness criterion using centripetal and extension profiles, and the conformation of these modules in aqueous solution was examined, showing that M1 has a helical structure and M5 has a sheet structure.

Exon-intron organization in genes of earthworm and vertebrate globins.

The structure of an invertebrate, intron-containing globin gene has been determined as part of a study of the evolution of hemoglobin and the 3' untranslated region of the Lumbricus gene is much longer than those of the genes for other hemoglobins and is similar to those found for myoglobin.

The seal myoglobin gene: an unusually long globin gene

The isolation and characterization of an additional diverged member of the globin gene family, the seal myoglobin gene, is described and it is shown that monomeric myoglobin, which diverged from haemoglobin about 600–800 Myr ago before the appearance of tetrameric haemoglobins8,9, is also specified by a gene containing two introns at positions precisely homologous toHaemoglobin introns.

Characterization and Expression of the Lucina pectinata Oxygen and Sulfide Binding Hemoglobin Genes

The gene expression levels of the clam Hbs showed a significant decrease of expression in the symbiont-containing tissue for those clams in a sulfide-poor environment, suggesting that the sulfide concentration may be involved in the regulation of these proteins.



The relationship between coding sequences and function in haemoglobin

To test the idea that coding sequences correspond to functional units of proteins, the relationship between the coding sequences of α and β globin genes and the corresponding parts of the complete, tetrameric haemoglobin molecule are considered.

Exons encode functional and structural units of chicken lysozyme.

The nucleotide sequence was determined for the chicken egg white lysozyme mRNA and for the exons of the gene together with their flanking intron regions to establish the relationship of exons to functional units of the enzyme.

Characterization of globin domains: heme binding to the central exon product.

These experiments confirm a prediction of W. Gilbert that the product of the central exon of the globin gene is a complete functional domain that binds heme tightly and specifically.

Comparison of cloned mouse alpha- and beta-globin genes: conservation of intervening sequence locations and extragenic homology.

  • A. LederH. Miller P. Leder
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1978
Though alpha and betamaj genes are encoded on different chromosomes, when their sequences are compared directly by visualization of heteroduplex structures, only one 150- to 200-base-pair segment of homology is recognized.

Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain.

The sequence confirms that the variable region gene lies on the DNA separated from the constant region of a mouse immunoglobulin light chain, the VlambdaII gene, andHypervariable region codons appear in the germ-line sequence.

Nucleation, rapid folding, and globular intrachain regions in proteins.

  • D. Wetlaufer
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1973
Possible means of testing the hypothesis that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules are discussed.