The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship

被引:120
作者
Martinez, Manuel [1 ]
Diaz, Isabel [1 ]
机构
[1] Univ Politecn Madrid, Ctr Biotecnol & Genom Plantas, Dpto Biotecnol, Lab Bioquim & Biol Mol,ETS Ingn Agronomos, E-28040 Madrid, Spain
关键词
D O I
10.1186/1471-2148-8-198
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Background: Cystatins and their putative targets, the families of cysteine proteinases C1A and C13 play key roles in plants. Comparative genomic analyses are powerful tools to obtain valuable insights into the conservation and evolution of the proteinases and their proteinaceous inhibitors, and could aid to elucidate issues concerning the function of these proteins. Results: We have performed an evolutionary comparative analysis of cysteine proteinases C1A and C13 and their putative inhibitors in representative species of different taxonomic groups that appeared during the evolution of the Viridiplantae. The results indicate that whereas C1A cysteine proteinases are present in all taxonomic groups, cystatins and C13 cysteine proteinases are absent in some basal groups. Moreover, gene duplication events have been associated to the increasing structural and functional complexities acquired in land plants. Conclusion: Comparative genomic analyses have provided us valuable insights into the conservation and evolution of the cystatin inhibitory family and their putative targets, the cysteine proteinases from families C1A and C13. Functionality of both families of proteins in plants must be the result of a coevolutionary process that might have occurred during the evolution of basal and land plants leading to a complex functional relationship among them.
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页数:12
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共 72 条
[1]   Structural and functional diversity within the cystatin gene family of Hordeum vulgare [J].
Abraham, Zamira ;
Martinez, Manuel ;
Carbonero, Pilar ;
Diaz, Isabel .
JOURNAL OF EXPERIMENTAL BOTANY, 2006, 57 (15) :4245-4255
[2]   Effects of potato plants expressing a barley cystatin on the predatory bug Podisus maculiventris via herbivorous prey feeding on the plant [J].
Alvarez-Alfageme, Fernando ;
Martinez, Manuel ;
Pascual-Ruiz, Sara ;
Castanera, Pedro ;
Diaz, Isabel ;
Ortego, Felix .
TRANSGENIC RESEARCH, 2007, 16 (01) :1-13
[3]   Inhibition of mammalian legumain by some cystatins is due to a novel second reactive site [J].
Alvarez-Fernandez, M ;
Barrett, AJ ;
Gerhartz, B ;
Dando, PM ;
Ni, JA ;
Abrahamson, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (27) :19195-19203
[4]  
Amon P, 1998, PLANT CELL, V10, P781
[5]   Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative [J].
Anisimova, Maria ;
Gascuel, Olivier .
SYSTEMATIC BIOLOGY, 2006, 55 (04) :539-552
[6]   Plant seed cystatins and their target enzymes of endogenous and exogenous origin [J].
Arai, S ;
Matsumoto, I ;
Emori, Y ;
Abe, K .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2002, 50 (22) :6612-6617
[7]  
Bailey TL., 1994, P 2 INT C INT SYST M, V2, P28
[8]   The S8 serine, C1A cysteine and Al aspartic protease families in Arabidopsis [J].
Beers, EP ;
Jones, AM ;
Dickerman, AW .
PHYTOCHEMISTRY, 2004, 65 (01) :43-58
[9]   Misreading of termination codons in eukaryotes by natural nonsense suppressor tRNAs [J].
Beier, H ;
Grimm, M .
NUCLEIC ACIDS RESEARCH, 2001, 29 (23) :4767-4782
[10]   AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell death [J].
Belenghi, B ;
Acconcia, F ;
Trovato, M ;
Perazzolli, M ;
Bocedi, A ;
Polticelli, F ;
Ascenzi, P ;
Delledonne, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (12) :2593-2604