Access the full text.
Sign up today, get DeepDyve free for 14 days.
(1989)
Purification and partial characterization of theRhizobium leguminosarumbiovar
S.L. Dellaporta, J. Wood, J.B. Hicks (1983)
A plant DNA minipreparation, version 2Plant Mol. Biol. Rep., 1
B. Fristensky, D. Horovitz, L.A. Hadwiger (1988)
cDNA sequences for pea disease resistance genesPlant Mol. Biol., 11
G. Truesdell, M. Dickman (1997)
Isolation of pathogen/stress-inducible cDNAs from alfalfa by mRNA differential displayPlant Molecular Biology, 33
H. Breiteneder, Fatima Ferreira, Karin Hoffmann-Sommergruber, C. Ebner, Michael Breitenbach, H. Rumpold, Dietrich Kraft, Otto Scheiner (1993)
Four recombinant isoforms of Cor a I, the major allergen of hazel pollen, show different IgE-binding properties.European journal of biochemistry, 212 2
Jong-Chin Huang, Fa-Cheng Chang, Co-Shine Wang (1997)
Characterization of a lily tapetal transcript that shares sequence similarity with a class of intracellular pathogenesis-related (IPR) proteinsPlant Molecular Biology, 34
Y. Yen, P. Green (1991)
Identification and Properties of the Major Ribonucleases of Arabidopsis thaliana.Plant physiology, 97 4
N. Midoh, M. Iwata (1996)
Cloning and characterization of a probenazole-inducible gene for an intracellular pathogenesis-related protein in rice.Plant & cell physiology, 37 1
R.C. Allen (1994)
Gel Electrophoresis of Proteins and Nucleic Acids
(1998)
Structure of Lupinus luteusgenes YPR-10.1a and YPR-10.1b encoding two homologous pathogenesis-related proteins of PR-10
G. Moiseyev, L. Fedoreyeva, Y. Zhuravlev, Elena Yasnetskaya, P. Jekel, J. Beintema (1997)
Primary structures of two ribonucleases from ginseng callusesFEBS Letters, 407
M. Saraste, P. Sibbald, A. Wittinghofer (1990)
The P-loop--a common motif in ATP- and GTP-binding proteins.Trends in biochemical sciences, 15 11
P.A. Bariola, P.J. Green (1997)
Plant Ribonucleases: Structure and Function
R. Hewick, M. Hunkapiller, L. Hood, W. Dreyer (1981)
A gas-liquid solid phase peptide and protein sequenator.The Journal of biological chemistry, 256 15
E. Bause (1983)
Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes.The Biochemical journal, 209 2
K. Hahlbrock, D. Scheel (1989)
Physiology and Molecular Biology of Phenylpropanoid Metabolism, 40
J. Hofsteenge (1977)
Ribonucleases: Structure and Function
K. Struhl (1989)
RibonucleasesCurrent Protocols in Molecular Biology, 8
G. Moiseyev, J. Beintema, L. Fedoreyeva, G. Yakovlev (2004)
High sequence similarity between a ribonuclease from ginseng calluses and fungus-elicited proteins from parsley indicates that intracellular pathogenesis-related proteins are ribonucleasesPlanta, 193
D. Crowell, M. John, D. Russell, R. Amasino (1992)
Characterization of a stress-induced, developmentally regulated gene family from soybeanPlant Molecular Biology, 18
I. Somssich, E. Schmelzer, P. Kawalleck, K. Hahlbrock (1988)
Gene structure and in situ transcript localization of pathogenesis-related protein 1 in parsleyMolecular and General Genetics MGG, 213
B. Fristensky, D. Horovitz, L. Hadwiger (1988)
cDNA sequences for pea disease resistance response genesPlant Molecular Biology, 11
E. Iturriaga, M. Leech, D. Barratt, Trevor Wang (2004)
Two ABA-responsive proteins from pea (Pisum sativum L.) are closely related to intracellular pathogenesis-related proteinsPlant Molecular Biology, 24
J. Antoniw, C. Ritter, W. Pierpoint, L. Loon (1980)
Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMVJournal of General Virology, 47
(1998)
Pathogenesis - related protein PR - 10 from white lupin . ( Sequence anouncement . )
Nica Borgese, Diego Aggujaro, Paola Carrera, G. Pietrini, Monique Bassetti (1996)
A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranesThe Journal of Cell Biology, 135
M. Geffen, M. Ven (2003)
A Structure for Requirements
S. Warner, R. Scott, J. Draper (1992)
Characterisation of a wound-induced transcript from the monocot asparagus that shares similarity with a class of intracellular pathogenesis-related (PR) proteinsPlant Molecular Biology, 19
T. Boller (1993)
Antimicrobial Functions of the Plant Hydrolases, Chitinase and ß-1,3-Glucanase
A. Aitken (1990)
Identification of protein consensus sequences : active site motifs, phosphorylation, and other post-translational modifications
M. Walter, J. Liu, J. Wünn, D. Hess (1996)
Bean ribonuclease-like pathogenesis-related protein genes (Ypr10) display complex patterns of developmental, dark-induced and exogenous-stimulus-dependent expression.European journal of biochemistry, 239 2
E. Bause (1983)
Structure requirements of N-glycosylation of proteinsBiochem. J., 209
H. Breiteneder, K. Pettenburger, A. Bito, R. Valenta, D. Kraft, H. Rumpold, O. Scheiner, M. Breitenbach (1989)
The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene.The EMBO Journal, 8
M. Walter, Jan-Wei Liu, C. Grand, C. Lamb, D. Hess (1990)
Bean pathogenesis-related (PR) proteins deduced from elicitor-induced transcripts are members of a ubiquitous new class of conserved PR proteins including pollen allergensMolecular and General Genetics MGG, 222
A. Bufe, M. Spangfort, H. Kahlert, M. Schlaak, W. Becker (2004)
The major birch pollen allergen, Bet v 1, shows ribonuclease activityPlanta, 199
I. Swoboda, K. Hoffmann‐Sommergruber, G. O’Riordain, O. Scheiner, E. Heberle‐Bors, Ó. Vicente (1996)
Bet v 1 proteins, the major birch pollen allergens and members of a family of conserved pathogenesis‐related proteins, show ribonuclease activity in vitroPhysiologia Plantarum, 96
J.P. Carr, D.F. Klessig (1989)
Genetic Engineering: Principles and Methods
(1995)
cDNA sequences encoding for two homologues of Lupinus luteus ( L . ) IPR - like proteins ( Accession No . X 79974 and X 79975 for LIR 18 A and LIR 18 B mRNAs respectively )
J. Sambrook, E. Fritsch, T. Maniatis (2001)
Molecular Cloning: A Laboratory Manual
U. Pfitzner, Arthur Pfitzner, Howard Goodman (1999)
Pathogenesis-related proteins in plantsCritical Reviews in Plant Sciences, 10
Gerrit Smit, Trudy Logman, M. Boerrigter, J. Kijne, B Lugtenberg (1989)
Purification and partial characterization of the Rhizobium leguminosarum biovar viciae Ca2+-dependent adhesin, which mediates the first step in attachment of cells of the family Rhizobiaceae to plant root hair tipsJournal of Bacteriology, 171
T. Boller (1987)
Developments in Plant Pathology
P. Mylona, M. Moerman, Wei-cai Yang, T. Gloudemans, Joel Kerckhove, A. Kammen, T. Bisseling, H. Franssen (1994)
The root epidermis-specific pea gene RH2 is homologous to a pathogenesis-related genePlant Molecular Biology, 26
C. Bréda, C. Sallaud, J. El-Turk, D. Buffard, I. Kozak, R. Esnault, A. Kondorosi (1996)
Defense reaction in Medicago sativa: a gene encoding a class 10 PR protein is expressed in vascular bundles.Molecular plant-microbe interactions : MPMI, 9 8
P. Matsudaira (1987)
Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.The Journal of biological chemistry, 262 21
B. Pasloske (2001)
Ribonuclease inhibitors.Methods in molecular biology, 160
A. Stintzi, T. Heitz, V. Prasad, S. Wiedemann-Merdinoglu, S. Kauffmann, P. Geoffroy, M. Legrand, B. Fritig (1993)
Plant 'pathogenesis-related' proteins and their role in defense against pathogens.Biochimie, 75 8
(1977)
The composition and nutritive value of lupin seed
S. Swart, T.J.J. Logman, G. Smit, B.J.J. Lugtenberg, J.W. Kijne (1994)
Purification and partial characterization of a glycoprotein from pea with receptor activity for rhicadhesin, an attachment protein for RhizobiacceaePlant Mol. Biol., 24
D. Wessel, U. Flügge (1984)
A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids.Analytical biochemistry, 138 1
L.C. van Loon, W.S. Pierpoint, T. Boller, V. Conejero (1994)
Recommendations for naming plant pathogenesis-related proteinsPlant Mol. Biol. Rep., 12
P. Vidhyasekaran (2004)
Hydroxyproline-Rich Glycoproteins
S. Attucci, S. Aitken, P. Gulick, Ragai Ibrahim (1995)
Farnesyl pyrophosphate synthase from white lupin: molecular cloning, expression, and purification of the expressed protein.Archives of biochemistry and biophysics, 321 2
S. Swart, Trudy Logman, G. Smit, B. Lugtenberg, J. Kijne (2004)
Purification and partial characterization of a glycoprotein from pea (Pisum sativum) with receptor activity for rhicadhesin, an attachment protein of RhizobiaceaePlant Molecular Biology, 24
G.P. Moiseyev, L.I. Fedoreyeva, Y.N. Zhuravlev, E. Yasnetskaya, P.A. Jekel, J.J. Beintema (1997)
Primary structures of two ribonucleases from ginseng calluses. New members of the PR-10 family of intracellular pathogenesis-related plant proteinsFEBS Lett., 407
D. Pless, W. Lennarz (1977)
Enzymatic conversion of proteins to glycoproteins.Proceedings of the National Academy of Sciences of the United States of America, 74 1
(1995)
Cloning and sequencing of Mald 1, the major allergen from apple
E. Ruoslahti, Pierschbacher (1987)
New perspectives in cell adhesion: RGD and integrins.Science, 238 4826
M. Gajhede, P. Osmark, Flemming Poulsen, H. Ipsen, Jørgen Larsen, R. Neerven, C. Schou, H. Løwenstein, M. Spangfort (1996)
X-ray and NMR structure of Bet v 1, the origin of birch pollen allergyNature Structural Biology, 3
A. Vaandrager, Erich Ehlert, T. Jarchau, S. Lohmann, H. Jonge (1996)
N-terminal Myristoylation Is Required for Membrane Localization of cGMP-dependent Protein Kinase Type II (*)The Journal of Biological Chemistry, 271
M. Vanek-Krebitz, K. Hoffmann‐Sommergruber, M. Machado, M. Susani, C. Ebner, D. Kraft, O. Scheiner, H. Breiteneder (1995)
Cloning and sequencing of Mal d 1, the major allergen from apple (Malus domestica), and its immunological relationship to Bet v 1, the major birch pollen allergen.Biochemical and biophysical research communications, 214 2
Matton Dp, N. Brisson (1989)
Cloning, expression, and sequence conservation of pathogenesis-related gene transcripts of potato.Molecular plant-microbe interactions : MPMI, 2 6
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
J. Sommer-Knudsen, A. Bacic, A. Clarke (1998)
Hydroxyproline-rich plant glycoproteinsPhytochemistry, 47
An abundant 17 kDa protein which was isolated and characterized from 10-day old healthy root tissue of white lupin (Lupinus albus) proved to have a high sequence similarity to pathogenesis-related proteins found in other species. Subsequently, a corresponding clone (LaPR-10) was identified in a cDNA library prepared from the same tissue that exhibited a high amino acid sequence similarity to a number of the PR-10 family proteins. The clone contains an open reading frame encoding a polypeptide of 158 amino acids, with a predicted molecular mass of 16 905 Da and an isoelectric point of 4.66. Southern blot analysis indicates that LaPR-10 is likely a single-copy gene, or a member of a small gene family. The clone was expressed in Escherichia coli, and its protein product was purified to near homogeneity. Both the native and the recombinant proteins were immunorecognized by antibodies raised against pea PR-10 proteins, and exhibited a ribonucleolytic activity against several RNA preparations, including lupin root total RNA. Characterization of its enzymatic properties indicates that the LaPR-10 protein belongs to the class II ribonucleases. We present evidence that the white lupin 17 kDa protein is constitutively expressed during all stages of root development and, to a lesser extent, in other plant parts. In addition, we demonstrate the presence, in the LaPR-10 amino acid sequence, of a number of motifs that are common to most PR-10 proteins, as well as a RGD motif that is shared only with the alfalfa SRG1 sequence.
Plant Molecular Biology – Springer Journals
Published: Oct 16, 2004
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.