Plant stress proteins of the thaumatin-like family discovered in animals

被引:51
作者
Brandazza, A
Angeli, S
Tegoni, M
Cambillau, C
Pelosi, P
机构
[1] Univ Pisa, Dipartimento Chim & Biotecnol Agrarie, I-56124 Pisa, Italy
[2] Architecture & Fonct Macromol Biol, F-13402 Marseille 20, France
关键词
thaumatin; stress protein; glucanase; Schistocerca gregaria; Locusta migratoria; Caenorhabditis elegans; Caenorhabditis briggsae;
D O I
10.1016/j.febslet.2004.07.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Thaumatin-like proteins (TLPs) are polypeptides of about 200 residues synthesized by plants in response to fungal infection. In addition to the exceptionally strong sweet taste exhibited by some members, they are also reported to be endowed with endo-beta-1,3-glucanase activity and alpha-amylase inhibiting properties. However, the detailed mechanism of their antifungal action is not completely understood. So far, TLPs have only been described in plants, with several members of the family expressed in the same species. Here, for the first time in animals, we report the identification of two genes encoding members of the thaumatin-like proteins family in the desert locust Schistocerca gregaria and show their expression in different parts of the body. Southern blot and Western blot experiments revealed the presence of orthologous genes and their expression products in the related species Locusta migratoria. A search through the available genomes yielded similar sequences in the nematode Caenorhabditis but not in Drosophild and other insects. A three-dimensional model of S. gregaria TLP suggests a glucanase function. As in plants, TLPs could play a defense role in insects against pathogens. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:3 / 7
页数:5
相关论文
共 20 条
[11]  
Kitajima S, 1999, J BIOCHEM, V125, P1, DOI 10.1093/oxfordjournals.jbchem.a022244
[12]   Crystal structure of tobacco PR-5d protein at 1.8 Å resolution reveals a conserved acidic cleft structure in antifungal thaumatin-like proteins [J].
Koiwa, H ;
Kato, H ;
Nakatsu, T ;
Oda, J ;
Yamada, Y ;
Sato, F .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 286 (04) :1137-1145
[13]   ELECTROBLOTTING OF MULTIPLE GELS - A SIMPLE APPARATUS WITHOUT BUFFER TANK FOR RAPID TRANSFER OF PROTEINS FROM POLYACRYLAMIDE TO NITROCELLULOSE [J].
KYHSEANDERSEN, J .
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 1984, 10 (3-4) :203-209
[14]   A molecular basis for the endo-β1,3-glucanase activity of the thaumatin-like proteins from edible fruits [J].
Menu-Bouaouiche, L ;
Vriet, C ;
Peumans, WJ ;
Barre, A ;
Van Damme, EJM ;
Rougé, P .
BIOCHIMIE, 2003, 85 (1-2) :123-131
[15]   Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites [J].
Nielsen, H ;
Engelbrecht, J ;
Brunak, S ;
vonHeijne, G .
PROTEIN ENGINEERING, 1997, 10 (01) :1-6
[16]   CRYSTAL-STRUCTURE OF A SWEET TASTING PROTEIN THAUMATIN-I, AT 1.65 ANGSTROM RESOLUTION [J].
OGATA, CM ;
GORDON, PF ;
DEVOS, AM ;
KIM, SH .
JOURNAL OF MOLECULAR BIOLOGY, 1992, 228 (03) :893-908
[17]  
ROUSSEL A, 1991, SILICON GRAPHICS GEO, V81, P77
[18]  
VANDERWEL H, 1972, EUR J BIOCHEM, V31, P221
[19]   IDENTIFICATION, PURIFICATION, AND CHARACTERIZATION OF PATHOGENESIS-RELATED PROTEINS FROM VIRUS-INFECTED SAMSUN NN TOBACCO-LEAVES [J].
VANLOON, LC ;
GERRITSEN, YAM ;
RITTER, CE .
PLANT MOLECULAR BIOLOGY, 1987, 9 (06) :593-609
[20]   Isolation of an antifungal thaumatin-like protein from kiwi fruits [J].
Wang, HX ;
Ng, TB .
PHYTOCHEMISTRY, 2002, 61 (01) :1-6