Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins.
Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.
Henrissat
B
B
Laboratoire de Biochimie et Technologie des Protéines, Institut National de la Recherche Agronomique, Nantes, France.
Popineau
Y
Y
Kader
J C
JC
D000595:Amino Acid Sequence; D052179:Antigens, Plant; D002352:Carrier Proteins; D008969:Molecular Sequence Data; D010940:Plant Proteins; D055315:Prolamins; D011506:Proteins; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D014908:Triticum / Q000737:chemistry*
D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; D055315:Prolamins; D011506:Proteins; C511920:lipid transfer proteins, plant