Literature DB >> 7360245

The relationship between coding sequences and function in haemoglobin.

W A Eaton.   

Abstract

Gilbert has suggested that the presence of intervening sequences in DNA, called introns, can speed evolution by allowing novel proteins to be constructed from the pieces of existing ones. This hypothesis further suggests that the coding sequences, called exons, correspond to functional parts of the protein. The most striking example so far is the case of the immunoglobulin gamma heavy chain, where the four polypeptide sequences corresponding to the four coding sequences form structurally and functionally distinct parts of the molecule. The relation between the three coding sequences of the beta globin gene and structure or function is not as obvious, but the central coding sequence does code for the part of the globin chain which forms the haem crevice. To further test the idea that coding sequences correspond to functional units of proteins we consider the relationship between the coding sequences of alpha and beta globin genes and the corresponding parts of the complete, tetrameric haemoglobin molecule.

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Year:  1980        PMID: 7360245     DOI: 10.1038/284183a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  13 in total

1.  Origin of a "bridge" intron in the gene for a two-domain globin.

Authors:  Y Naito; C K Riggs; T L Vandergon; A F Riggs
Journal:  Proc Natl Acad Sci U S A       Date:  1991-08-01       Impact factor: 11.205

Review 2.  Allostery and cooperativity revisited.

Authors:  Qiang Cui; Martin Karplus
Journal:  Protein Sci       Date:  2008-06-17       Impact factor: 6.725

3.  Foldons, protein structural modules, and exons.

Authors:  A R Panchenko; Z Luthey-Schulten; P G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  1996-03-05       Impact factor: 11.205

4.  Do exons code for structural or functional units in proteins?

Authors:  T W Traut
Journal:  Proc Natl Acad Sci U S A       Date:  1988-05       Impact factor: 11.205

5.  Protein dynamics in minimyoglobin: is the central core of myoglobin the conformational domain?

Authors:  E E Di Iorio; W Yu; C Calonder; K H Winterhalter; G De Sanctis; G Falcioni; F Ascoli; B Giardina; M Brunori
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-01       Impact factor: 11.205

6.  The relationship between coding sequences and function in some heme binding proteins.

Authors:  P Argos; M G Rossmann
Journal:  J Mol Evol       Date:  1980-12       Impact factor: 2.395

7.  Identification of a recently evolved goat embryonic beta-globin pseudogene which retains transcriptional activity in vitro.

Authors:  S G Shapiro; J B Lingrel
Journal:  Mol Cell Biol       Date:  1984-10       Impact factor: 4.272

8.  The primary structures of two leghemoglobin genes from soybean.

Authors:  J J Hyldig-Nielsen; E O Jensen; K Paludan; O Wiborg; R Garrett; P Jørgensen; K A Marcker
Journal:  Nucleic Acids Res       Date:  1982-01-22       Impact factor: 16.971

Review 9.  The thalassemias: molecular mechanisms of human genetic disease.

Authors:  R A Spritz; B G Forget
Journal:  Am J Hum Genet       Date:  1983-05       Impact factor: 11.025

10.  Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.

Authors:  E A Robey; S R Wente; D W Markby; A Flint; Y R Yang; H K Schachman
Journal:  Proc Natl Acad Sci U S A       Date:  1986-08       Impact factor: 11.205

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