Peptide promiscuity: An evolutionary concept for plant defense

被引：107

作者：

Franco, Octavio Luiz ^{[1
]}

机构：

[1] Univ Catolica Brasilia, Ctr Anal Prote & Bioquim, Programa Posgrad Ciencias Genom & Biotecnol, BR-70790160 Brasilia, DF, Brazil

来源：

FEBS LETTERS | 2011年 / 585卷 / 07期

关键词：

Peptide evolvability; Protein promiscuity; Plant defense; Defensins; Cyclotides; ANTIMICROBIAL PEPTIDES; CATALYTIC PROMISCUITY; KALATA B1; ANTIFUNGAL; IDENTIFICATION; CYCLOTIDES; SEEDS; EVOLVABILITY; EXPRESSION; PROTEINS;

D O I：

10.1016/j.febslet.2011.03.008

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：

The phenomenon of protein promiscuity, in which multiple functions are associated with a single peptide structure, has gained attention in several research fields, including the plant defense field. With this in mind, this report intends to link various plant defense peptides with common scaffolds (defensins, cyclotides and 2S albumins), and multiple activities with the processes of promiscuity generation and protein evolvability. This link seems to create an efficient system of plant defense against insect pests and pathogens, and is thus essential to plant survival and evolution. This review also identifies future possibilities for the use of peptide promiscuity in designing novel drugs and synthetic biotechnological products. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：995 / 1000

页数：6

共 49 条

[1] The mode of antifungal action of plant, insect and human defensins [J].

Aerts, A. M. ;

Francois, I. E. J. A. ;

Cammue, B. P. A. ;

Thevissen, K. .

CELLULAR AND MOLECULAR LIFE SCIENCES, 2008, 65 (13) :2069-2079

[2] The 'evolvability' of promiscuous protein functions [J].

Aharoni, A ;

Gaidukov, L ;

Khersonsky, O ;

Gould, SM ;

Roodveldt, C ;

Tawfik, DS .

NATURE GENETICS, 2005, 37 (01) :73-76

[3]

Azzaoui K, 2007, CHEMMEDCHEM, V2, P874, DOI 10.1002/cmdc.200700036

[4] What makes an enzyme promiscuous? [J].

Babtie, Ann ;

Tokuriki, Nobuhiko ;

Hollfelder, Florian .

CURRENT OPINION IN CHEMICAL BIOLOGY, 2010, 14 (02) :200-207

[5] The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins [J].

Bakan, B. ;

Hamberg, M. ;

Larue, V. ;

Prange, T. ;

Marion, D. ;

Lascombe, M. -B. .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2009, 390 (03) :780-785

[6]

Belarmino LC, 2010, CURR PROTEIN PEPT SC, V11, P195

[7] Compensatory Mutations Restore Fitness during the Evolution of Dihydrofolate Reductase [J].

Brown, Kyle M. ;

Costanzo, Marna S. ;

Xu, Wenxin ;

Roy, Scott ;

Lozovsky, Elena R. ;

Hartl, Daniel L. .

MOLECULAR BIOLOGY AND EVOLUTION, 2010, 27 (12) :2682-2690

[8] Molecular signatures-based prediction of enzyme promiscuity [J].

Carbonell, Pablo ;

Faulon, Jean-Loup .

BIOINFORMATICS, 2010, 26 (16) :2012-2019

[9] Plant defensins-Prospects for the biological functions and biotechnological properties [J].

Carvalho, Andre de Oliveira ;

Gomes, Valdirene Moreira .

PEPTIDES, 2009, 30 (05) :1007-1020

[10] Evolvability and Single-Genotype Fluctuation in Phenotypic Properties: A Simple Heteropolymer Model [J].

Chen, Tao ;

Vernazobres, David ;

Yomo, Tetsuya ;

Bornberg-Bauer, Erich ;

Chan, Hue Sun .

BIOPHYSICAL JOURNAL, 2010, 98 (11) :2487-2496

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