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Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins.

ABSTRACT: 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.

SUBMITTER: Henrissat B

PROVIDER: S-EPMC1135326 | biostudies-other | 1988 Nov

REPOSITORIES: biostudies-other

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The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs).

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