Heavy Metal-Binding Peptides and Proteins in Plants. A Review

1999 ◽  
Vol 64 (7) ◽  
pp. 1057-1086 ◽  
Author(s):  
Pavel Kotrba ◽  
Tomáš Macek ◽  
Tomáš Ruml

In plants, two kinds of specific metal-binding peptides or proteins are synthesized. Plant metallothioneins (MTs) and MT-like proteins are cysteine-rich translation products of genes inducible in tissue-specific manner during embryogenesis and plant development. In addition, differential expression of MT-like protein genes could be due to variation of external heavy metal concentrations (especially of Cu2+ and Fe2+), influence of various stress factors (heat shock, sucrose starvation, oxidative stress, wounding, plant pathogens). The principal role of plant MTs and MT-like proteins seems to be in homeostasis of essential transition metals rather than in metal detoxification. Phytochelatins (PCs) have general structure (γ-Glu-Cys)n-Xaa, where n = 2-11 and Xaa amino acids Gly, β-Ala, Ser, and Glu which depend on the species; the des-Xaa forms of PC also exist. PCs are synthesized in plants and some yeasts by a constitutive enzyme phytochelatin synthase (active only in the presence of free heavy metal ion) from glutathione or its anologue. Despite the PC capability of forming complexes with transition metal ions (their role in metal homeostasis could not be excluded) and virtually prominent role in Cd2+ detoxification within plant cell, there is no evidence that elevated production of PCs may contribute to differential tolerance and/or could be responsible for the resistance to toxic metals. A review with 172 references.

FEBS Letters ◽  
1986 ◽  
Vol 205 (1) ◽  
pp. 47-50 ◽  
Author(s):  
E. Grill ◽  
W. Gekeler ◽  
E.-L. Winnacker ◽  
H.H. Zenk

2005 ◽  
Vol 100 (6) ◽  
pp. 593-599 ◽  
Author(s):  
Kazumasa Hirata ◽  
Naoki Tsuji ◽  
Kazuhisa Miyamoto

1999 ◽  
Vol 65 (3) ◽  
pp. 1092-1098 ◽  
Author(s):  
Pavel Kotrba ◽  
Lucie Dolečková ◽  
Víctor de Lorenzo ◽  
Tomas Ruml

ABSTRACT Metal binding peptides of sequences Gly-His-His-Pro-His-Gly (named HP) and Gly-Cys-Gly-Cys-Pro-Cys-Gly-Cys-Gly (named CP) were genetically engineered into LamB protein and expressed in Escherichia coli. The Cd2+-to-HP and Cd2+-to-CP stoichiometries of peptides were 1:1 and 3:1, respectively. Hybrid LamB proteins were found to be properly folded in the outer membrane ofE. coli. Isolated cell envelopes of E. colibearing newly added metal binding peptides showed an up to 1.8-fold increase in Cd2+ binding capacity. The bioaccumulation of Cd2+, Cu2+, and Zn2+ by E. coli was evaluated. Surface display of CP multiplied the ability of E. coli to bind Cd2+ from growth medium fourfold. Display of HP peptide did not contribute to an increase in the accumulation of Cu2+ and Zn2+. However, Cu2+ ceased contribution of HP for Cd2+accumulation, probably due to the strong binding of Cu2+ to HP. Thus, considering the cooperation of cell structures with inserted peptides, the relative affinities of metal binding peptide and, for example, the cell wall to metal ion should be taken into account in the rational design of peptide sequences possessing specificity for a particular metal.


ChemInform ◽  
2010 ◽  
Vol 30 (42) ◽  
pp. no-no
Author(s):  
Pavel Kotrba ◽  
Tomas Macek ◽  
Tomas Ruml

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