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Garratt, Richard; Oliva, Glaucius; Caracelli, Ignez; Leite, Adilson; Arruda, Paulo

Studies of the zein‐like α‐prolamins based on an analysis of amino acid sequences: Implications for their evolution and three‐dimensional structure

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  • Media type: E-Article
  • Title: Studies of the zein‐like α‐prolamins based on an analysis of amino acid sequences: Implications for their evolution and three‐dimensional structure
  • Contributor: Garratt, Richard; Oliva, Glaucius; Caracelli, Ignez; Leite, Adilson; Arruda, Paulo
  • Published: Wiley, 1993
  • Published in: Proteins: Structure, Function, and Bioinformatics, 15 (1993) 1, Seite 88-99
  • Language: English
  • DOI: 10.1002/prot.340150111
  • ISSN: 0887-3585; 1097-0134
  • Origination:
  • Footnote:
  • Description: Abstractα‐Prolamins are the major seed storage proteins of species of the grass tribe Andropogonea. They are unusually rich in glutamine, proline, alanine, and leucine residues and their sequences show a series of tandem repeats presumed to be the result of multiple intragenic duplication. Two new sequences of α‐prolamin clones from Coix (pBCX25.12 and pBCX25.10) are compared with similar clones from maize and Sorghum in order to investigate evolutionary relationships between the repeat motifs and to propose a schematic model for their three‐dimensional structure based on hydrophobic membrane‐helix propensities and helical “wheels.” A scheme is proposed for the most recent events in the evolution of the central part of the molecule (repeats 3 to 8) which involves two partial intragenic duplications and in which contemporary odd‐numbered and even‐numbered repeats arise from common ancestors, respectively. Each pair of repeats is proposed to form an antiparallel α‐helical hairpin and that the helices of the molecule as a whole are arranged on a hexagonal net. The majority of helices show six faces of alternating hydrophobic and polar residues, which give rise to intersticial holes around each helix which alternate in chemical character. The model is consistent with proteins which contain different numbers of repeats, with oligomerization and with the dense packaging of α‐prolamins within the protein body of the seed endosperm. © 1993 Wiley‐Liss, Inc.