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Bet v 1 proteins, the major birch pollen allergens and members of a family of conserved pathogenesis‐related proteins, show ribonuclease activity in vitro
Author(s) -
Swoboda Ines,
HoffmannSommergruber Karin,
O'Ríordáin Gabriel,
Scheiner Otto,
HeberleBors Erwin,
Vicente Oscar
Publication year - 1996
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1996.tb00455.x
Subject(s) - ribonuclease , biology , pathogenesis related protein , biochemistry , protein family , conserved sequence , gene , rna , recombinant dna , microbiology and biotechnology , peptide sequence , gene expression
The Bet v. 1 gene family of birch encodes the major pollen allergens as well as pathogenesis‐related (PR) proteins that are induced by microbes in somatic tissues. These PR proteins belong to a group of conserved intracellular defense‐related proteins that have been termed ‘ribonuclease‐like’ PR proteins, on the basis of the partial sequence homology observed between PR1, a Bet v 1‐homologue from parsley, and a recently characterized ginseng ribonuclease. However, this enzymatic activity has not yet been demonstrated, not for any of the members of this family of PR proteins, nor for the related pollen allergens. We have investigated the possible nuclease activity of Bet v 1 using apparently homogeneous preparations of natural Bet v 1 purified from birch pollen, and a recombinant non‐fusion protein purified from E. coli extracts. We report here that Bet v 1 proteins indeed possess an intrinsic ribonucleolytic activity as they can digest different RNA substrates in vitro, but show no activity on single or double‐stranded DNA.