Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/75429
Type: Artigo de periódico
Title: STUDIES OF THE ZEIN-LIKE ALPHA-PROLAMINS BASED ON AN ANALYSIS OF AMINO-ACID-SEQUENCES - IMPLICATIONS FOR THEIR EVOLUTION AND 3-DIMENSIONAL STRUCTURE
Author: GARRATT, R
OLIVA, G
CARACELLI, I
LEITE, A
ARRUDA, P
Abstract: Alpha-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 alpha-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 alpha-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 alpha-prolamins within the protein body of the seed endosperm.
Subject: ALPHA-ZEINS
ALPHA-KAFIRINS
ALPHA-COIXINS
STRUCTURE PREDICTION
GENE DUPLICATION
HELIX PACKING
QUATERNARY STRUCTURE
Editor: Wiley-liss
Rights: fechado
Identifier DOI: 10.1002/prot.340150111
Date Issue: 1993
Appears in Collections:Unicamp - Artigos e Outros Documentos

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