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PMID: 3214430 Published · ppublish English Comparative Study Journal Article

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

The Biochemical journal ·Vol. 255 ·No. 3 ·1988-11-01 ·Pages 901-5

Henrissat B, Popineau Y, Kader JC

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.

MeSH Terms
Amino Acid Sequence Antigens, Plant Carrier Proteins Molecular Sequence Data Plant Proteins Prolamins Proteins Sequence Homology, Nucleic Acid Species Specificity Triticum/chemistry
Chemicals
Antigens, Plant Carrier Proteins Plant Proteins Prolamins Proteins lipid transfer proteins, plant
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Henrissat B
Laboratoire de Biochimie et Technologie des Protéines, Institut National de la Recherche Agronomique, Nantes, France.
Popineau Y
Kader J C
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2550901
Published
1988-11-01
Pages
901-5
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1135326
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2550901 PMC Full Text View journal details
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