Bean pathogenesis-related (PR) proteins deduced from elicitor-induced transcripts are members of a ubiquitous new class of conserved PR proteins including pollen allergens

Abstract

We have searched for induced transcripts in a cDNA library derived from bean cell supension cultures treated with an elicitor from Colletotrichum lindemuthianum. Six independently isolated cDNAs corresponding to rapidly induced small mRNAs have been classified by their DNA sequence and slightly different induction behaviour into two groups. 5'- and 3'-untranslated regions exhibit little similarity, but the deduced small acidic proteins designated PvPR1 and PvPR2 are 89% identical. No relationship was found with the well-characterized PR1 proteins from tobacco. However, the PvPR proteins are closely related to pI49 in pea (64% identity), pSTH2 in potato (41% identity) and PcPR1-1 in parsley (39% identity), which are also induced in response to elicitor or microbial attack. Moreover, a major pollen allergen in birch (BetvI) has a 44% identity with PvPR1 proteins. These similarities establish a ubiquitous class of conserved defense-related proteins and suggest a common yet still unknown function. Southern blot analysis indicates that PvPR protein gene organization is highly complex with an estimated copy number of more than 12 genes.

The developmental expression of the asparagus intracellular PR protein (AoPR1) gene correlates with sites of phenylpropanoid biosynthesis

“…The AoPR1 gene (Warner et al, 1992) derived from an asparagus wound-induced messenger RNA population (Harikrishna et al, 1991) shares homology with a new class of pathogenesis-related proteins (Walter et al, 1990). Several lines of evidence suggest that this group of PR proteins are intraceliular (Somssich et al, 1988;Warner et al, 1992) and thus differ from the 'classical' acidic PR proteins described from tobacco which are generally extracellular .…”

The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related

“…Examples are Bet v 1 from birch (Swoboda et al, 1996), Mal d 1 from apple (Malus domestica; Vanek-Krebitz et al, 1995), Pru ar 1 from apricot (Prunus armeniaca), Pru av 1 from cherry (Neudecker et al, 2001), and Dau c 1 from carrot (Daucus carota; Yamamoto et al, 1997). On the other hand, several PR-10 proteins are up-regulated upon pathogen infection (Walter et al, 1990;Breda et al, 1996;Pü hringer et al, 2000;Park et al, 2004;Liu et al, 2005), have a direct and selective antifungal activity, or accumulate in overwintering organs of tree species, suggesting a key role in selective defense mechanisms against microbes and fungi and in protecting plants from abiotic stresses (Yu et al, 2000;Flores et al, 2002;Chadha and Das, 2006). In addition, a number of PR-10 proteins are constitutively expressed at different plant developmental stages and/ or in different tissues and organs, such as in seeds, roots (Sikorski et al, 1999), flowers, and senescent leaves (Breiteneder et al, 1989;Crowell et al, 1992;Barrat and Clark, 1993;Vanek-Krebitz et al, 1995;Sikorski et al, 1999), suggesting a role for PR-10 proteins also in developmental regulation.…”

Amino acid sequence of proteins induced in Fe-deficient stressed alfalfa (Medicago sativaL.) roots

“…I was compared with the primary structure of pea ABRI7 (Iturriaga et al 1994) and kidney bean with that of PvPRI (Walter et al 1990). Peptide No.2 was compared with those of alfalfa SRGI (Truesdell and Dickman 1997), alfalfa MsPRlO-1 (Breda et al 1996) and kidney bean PvPR2 (Walter et al 1990). Peptide No.3 was compared with the primary structure of pea (White and Zilinskas 1991) and maize (Canon and Scandalios 1989) cytosolic Cu,Zn-SOD.…”