Evolutionary Relationships Among Proteins in the Phytohemagglutinin-arcelin-alpha-amylase Inhibitor Family of the Common Bean and Its Relatives

Overview

Journal Plant Mol Biol

Date 1994 Nov 1

PMID 7811969

Citations 31

Authors

T E Mirkov

J M Wahlstrom

K Hagiwara

S Kjemtrup

M J Chrispeels

Affiliations

Soon will be listed here.

Abstract

The common bean, Phaseolus vulgaris, contains a family of defense proteins that comprises phytohemagglutinin (PHA), arcelin, and alpha-amylase inhibitor (alpha AI). Here we report eight new derived amino acid sequences of genes in this family obtained with either the polymerase chain reaction using genomic DNA, or by screening cDNA libraries made with RNA from developing beans. These new sequences are: two alpha AI sequences and arcelin-4 obtained from a wild accession of P. vulgaris that is resistant to the Mexican bean weevil (Zabrotes subfasciatus) and the bean weevil (Acanthoscelides obtectus); an alpha AI sequence from the related species P. acutifolius (tepary bean); a PHA and an arcelin-like sequence from P. acutifolius; an alpha AI-like sequence from P. maculatus; and a PHA sequence from an arcelin-5 type P. vulgaris. A dendrogram of 16 sequences shows that they fall into the three identified groups: phytohemagglutinins, arcelins and alpha AIs. A comparison of these derived amino acid sequences indicates that one of the four amino acid residues that is conserved in all legume lectins and is required for carbohydrate binding is absent from all the arcelins; two of the four conserved residues needed for carbohydrate binding are missing from all the alpha AIs. Proteolytic processing at an Asn-Ser site is required for the activation of alpha AI, and this site is present in all alpha AI-like sequences; this processing site is also found at the same position in certain arcelins, which are not proteolytically processed. The presence of this site is therefore not sufficient for processing to occur.

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