Pavel Kotrba

Publications (36) View all

• Source

  Available from: Lenka Svabova

  Article: Vrbová M., Kotrba, P., Horáček, J., Smýkal, P., Švábová, L., Větrovcová M., Smýkalová I., Griga, M. (2012) Enhanced accumulation of Cadmium in Linum ussitatissimum L. plants due to overproduction of metallothionein α-domain as a fusion to β-glucuronidase gene protein. PCTOC, DOI: 10.1007/s11240-012-0239-1

  Miroslava Vrbová, Pavel Kotrba, Jiří Horáček, Petr Smýkal, Lenka Švábová, Martina Větrovcová, Iva Smýkalová, Miroslav Griga
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  ABSTRACT: Enhanced accumulation of cadmium in Linum usitatissimum L. plants due to overproduction of metallothionein α-domain as a fusion to β-glucuronidase protein
  01/2012;
• Chapter: Transgenic Approaches to Improve Phytoremediation of Heavy Metal Polluted Soils

  Pavel Kotrba, Martina Mackova, Tomas Macek
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  ABSTRACT: Use of plants to remediate soil contaminated with heavy metals has received an increasing attention during the last decade. Bioremediation using living plant species, referred to as phytoremediation, covers several different strategies, of which bioremediation employs phytoextraction, rhizofiltration, phytostabilization, and phytovolatilization. High efficiency, low cost, and easy operation make phytoremediation an important alternative to current physicochemical methods. Although, a number of metal-hyperaccumulating plant species have been identified, they have little significance in direct application because of their slow growth, low biomass, and intense interaction with a specific habitat. The phytoremediation potential of plants with well-established agricultural properties and high-biomass yield can be substantially improved by genetic manipulations. The transgenic approaches involve implementation of heterologous metal transporters, centrally important in metal uptake, compartmentalization and/or translocation to organs, improved production of intracellular metal-detoxifying chelators, and (over)production of novel enzymes. Efforts are also being directed to obtain better molecular insights into metallomics and physiology of hyperaccumulating plants, which is likely to provide candidate genes suitable for phytoremediation. Although substantial progress has been made, further efforts require interdisciplinary approach and, more so, field trials are needed to assess the risk of genetic pollution and underlying economics. Here, we discuss the evidence supporting suitability and prospects of transgenic approaches in phytoremediation of heavy metal-contaminated soils. KeywordsBioremediation-Decontamination-Genetic engineering-Phytoextraction-Phytovolatilization
  08/2011: pages 409-438;
• Article: The ptsI gene encoding enzyme I of the phosphotransferase system of Corynebacterium glutamicum.

  P Kotrba, M Inui, H Yukawa
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  ABSTRACT: The phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS) is widespread among bacteria where it mediates carbohydrate uptake and often serves in carbon control. Here we present cloning and analysis of the monocistronic ptsI gene of Corynebacterium glutamicum R, which encodes PTS Enzyme I (EI). EI catalyzes the first reaction of PTS and the reported ptsI was shown to complement the corresponding defect in Escherichia coli. The deduced 59.2-kDa EI of 564 amino acids shares more than 50% homology with EIs from Bacillus stearothermophilus, Bacillus subtilis, and Lactobacillus sake. Chromosomal inactivation of ptsI demonstrated that EI plays an indispensable role in PTS of C. glutamicum R and this system represents a dominant sugar uptake system. Cellobiose was only transported and utilized in adaptive mutants of C. glutamicum R. Cellobiose transport was also found to be PTS-dependent and repressed by PTS sugar glucose.
  Biochemical and Biophysical Research Communications 01/2002; 289(5):1307-13. · 2.48 Impact Factor
• Article: Bacterial phosphotransferase system (PTS) in carbohydrate uptake and control of carbon metabolism.

  P Kotrba, M Inui, H Yukawa
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  ABSTRACT: More than 20 carbohydrates may be transported into the bacterial cell by the phosphoenopyruvate:carbohydrate phosphotransferase system (PTS) that is widely spread among bacteria. The PTS consists of two cytoplasmic energy-coupling proteins (Enzyme I and HPr) and a range of carbohydrate-specific Enzymes II, which catalyze concomitant carbohydrate translocation and phosphorylation. The phosphorylation status of PTS components reflects the availability of carbohydrates and the energy conditions of the cell. In many bacteria, PTS and the associated proteins convert this information to signals, which transduced through different mechanisms lead to phenomena of catabolite repression, inducer control or chemotaxis. These features of PTS provide bacteria with an integrated system, which assures optimal utilization of carbohydrates in complex environments. Furthermore, some bacteria evolved parallel systems that serve a regulatory functions, but apparently do not catalyze the carbohydrate transport. Here we review the findings that recently advanced the understanding of various aspects of PTS-dependent carbohydrate transport and regulation of bacterial catabolism.
  Journal of Bioscience and Bioengineering 02/2001; 92(6):502-17. · 1.79 Impact Factor
• Source

  Available from: ncbi.nlm.nih.gov

  Article: Enhanced bioaccumulation of heavy metal ions by bacterial cells due to surface display of short metal binding peptides.

  P Kotrba, L Dolecková, V de Lorenzo, T Ruml
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  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 of E. coli. Isolated cell envelopes of E. coli bearing 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.
  Applied and Environmental Microbiology 04/1999; 65(3):1092-8. · 3.83 Impact Factor