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1
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
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Localization of acid phosphatase activity in the apoplast of root nodules of pea [Pisum sativum]

100%
Sujkowska M., Borucki W., Golinowski W.
Acta Societatis Botanicorum Poloniae
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2006
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tom 75
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nr 1
33-38
Changes in the activity of acid phosphatase (AcPase) in the apoplast of pea root nodule were investigated. The activity was determined using lead and cerium methods. The results indicated a following sequence of AcPase activity appearance during the development of the infection thread: 1) low AcPase activity appears in the outer part of cells of symbiotic bacteria; 2) bacteria show increased AcPase activity, and the enzyme activity appears in the thread walls; 3) activity exhibits also matrix of the infection thread; 4) bacteria just before their release from the infection threads show high AcPase activity; 5) AcPase activity ceases after bacteria transformation into bacteroids. The increase in bacterial AcPase activity may reflect a higher demand for inorganic phosphorus necessary for propagation of the bacteria within the infection threads and/or involved in bacteria release from the infection threads.
2

Studies on the competition of Rhizobia strains in soil

100%
Kowalczuk E., Lorkiewicz Z.
Polish Journal of Soil Science
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1997
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tom 30
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nr 2
3
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Localization of (homo)glutathione in effective and partially effective root nodules of Medicago truncatula root nodules

84%
Bederska M., Borucki W.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 3
4

Symbiotic nitrogen fixation in narrow-leafed lupin investigated with differential screening and cDNA arrays

84%
Zmienko A., Legocki A. B., Figlerowicz M., Podkowinski J.
Biological Letters
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2005
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tom 42
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nr 2 Spec.Vol.
5
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Medicago truncatula ABC transporter modulates nodulation efficiency

67%
Jarzyniak K., Banasiak J., Szewczak A., Jasinski M.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 3
6
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
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Localization of expansin-like protein in apoplast of pea [Pisum sativum L.] root nodules during interaction with Rhizobium leguminosarum bv. viciae 248

67%
Sujkowska M., Borucki W., Golinowski W.
Acta Societatis Botanicorum Poloniae
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2007
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tom 76
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nr 1
During nodule development on pea roots, apoplast undergoes changes in activity of plant cell wall proteins such as expansins (EXPs). Because the accumulation of EXP protein has been correlated with the growth of various plant organs, we investigated using Western Blot and immunolocalization studies with antibody against PsEXP1, whether this protein was accumulated in the expanding cells of nodule. Immunoblot results indicated the presence of a 30-kDa band specific for pea root nodules. The EXP proteins content rose during growth of pea root nodules. Expansin(s) protein was localized in nodule apoplast as well as in the infection thread walls. The enhanced amount of expansin-like proteins in meristematic part of nodule, root and shoot was shown. The localization of this protein in the meristematic cell walls can be related to the loosening of plant cell wall before cell enlargement. Both, plant cell enlargement and infection thread growth require activity of expansin(s). Possible involvement of EXPs in the process of pea root nodule development is also discussed.
7

Alteration of O-specific polysaccharide structure of symbiotically defective Mesorhizobium loti mutant 2213.1 derived from strain NZP2213

67%
Turska-Szewczuk A., Pietras H., Borucki W., Russa R.
Acta Biochimica Polonica
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2008
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tom 55
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nr 1
Mesorhizobium loti mutant 2213.1 derived from the wild-type strain NZP2213 by Tn5 mutagenesis showed impaired effectiveness of symbiosis with the host plant Lotus corniculatus (Turska-Szewczuk et al., 2007 Microbiol Res, in press). The inability of lipopolysaccharide (LPS) isolated from the mutant 2213.1 strain or de-O-acetylated LPS of the parental cells to inactivate phage A1 particles implicated alterations in the LPS structure. The O-specific polysaccharide of the mutant was studied by chemical analyses along with  1H and  13C NMR spectroscopy, which clearly confirmed alterations in the O-chain structure. 2D NMR data showed that the mutant O-polysaccharide consists of a tetrasaccharide repeating unit containing non-substituted as well as O-acetylated or O-methylated 6-deoxytalopyranose residues. Additionally, an immunogold assay revealed a reduced number of gold particles on the mutant bacteroid cell surface, which could result from both a diminished amount of an O-antigenic determinant in mutant LPS and modifications of structural epitopes caused by alterations in O-acetylation or O-methylation of sugar residues. Western immunoblot assay of alkaline de-O-acetylated lipophilic M. loti NZP2213 LPS showed no reactivity with homologous serum indicating a role of O-acetyl groups in its O-specificity.
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