Wyniki wyszukiwania

1

The plant Nudix hydrolase family

100%

Kraszewska E.

Acta Biochimica Polonica

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2008

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tom 55

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nr 4

663-671

Nudix hydrolases are a family of proteins defined by a conserved amino-acid sequence GX5-EX7REUXEEXGU, where U is a hydrophobic residue. These enzymes are widely distributed among all classes of organisms and catalyze, with varying degrees of substrate specificity, the hydrolysis of a variety of nucleoside diphosphate derivatives: nucleoside di- and triphosphates and their oxidized forms, dinucleoside polyphosphates, nucleotide sugars, NADH, coenzyme A and the mRNA cap. Nudix proteins are postulated to control the cellular concentration of these compounds. The genome of the model plant Arabidopsis thalianacontains 29 genes coding for putative Nudix hydrolases. Recently, several Arabidopsis Nudix genes have been cloned and their products characterized. This review summarizes current knowledge on these plant enzymes and discusses their possible cellular functions.

2

A mechanism that cuuples DNA transposition to cell differentiation ( Hypothesis)

63%

Buchowicz J., Kraszewska E.

Acta Biochimica Polonica

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1984

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tom 31

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nr 1

3

Zastosowanie metody "kruchych pokryć" do badania naprężeń w kopytach

63%

Kraszewska E., Charasz A.

Przegląd Skórzany

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1986

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tom 41

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nr 11

4

Nudix hydrolase PA5176 is linked to Rhamnolipids production in Pseudomonas aeruginosa

63%

Ziecina M., Kraszewska E.

Postępy Mikrobiologii. Suplement

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2017

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tom 56

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nr 1

5

Transient and stable transformation of wheat with DNA preparations delivered by a biolistic method

51%

Dobrzanska M., Krysiak C., Kraszewska E.

Acta Physiologiae Plantarum

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1997

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tom 19

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nr 3

An optimized procedure for transformation of wheat with the use of a Biolistic Particle Delivery System PDS 1000/He to deliver foreign DNA is described in detail. The bacterial uidA and bar genes (both driven by plant promoters) were utilized as the reporter and selectable marker genes, respectively. Moderately high gas pressure appeared to be most important to achieve the highest level of transient GUS expression in target tissues. There was, however, no apparent correlation between transient and stable GUS expression. The presence of telomeric DNA sequences in an uidA gene-containing vector did not influence transient GUS expression but, apparently, prevented its stable expression. Mechanical lesions caused by the bombardment (tungsten particles) seemed to be less severe when embryo- derived calli, instead of freshly excised immature embryos, were used as the target tissue. The limited ability of callus cells for regeneration, together with a restricted number of cells that receive the foreign DNA by particle bombardment, result in a low efficiency of wheat stable transformation.

6

Mutational analysis of the AtNUDT7 Nudix hydrolase from Arabidopsis thaliana reveals residues required for protein quarternary structure formation and activity

39%

Olejnik K., Plochocka D., Grynberg M., Goch G., Gruszecki W. I., Basinska T., Kraszewska E.

Acta Biochimica Polonica

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2009

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tom 56

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nr 2

291-300

Arabidopsis thaliana AtNUDT7, a homodimeric Nudix hydrolase active on ADP-ribose and NADH, exerts negative control on the major signaling complex involved in plant defense activation and programmed cell death. The structural and functional consequences of altering several amino-acid residues of the AtNUDT7 protein have been examined by site-directed mutagenesis, far-UV circular dichroism (CD), attenuated total reflection-Fourier transform infrared (ATR-FTIR) and photon correlation (PCS) spectroscopy, biochemical analysis and protein-protein interaction studies. Alanine substitutions of F73 and V168 disallowed dimer formation. Both the F73A- and V168A-mutated proteins displayed no observable enzymatic activity. Alanine substitution of the V69 residue did not significantly alter the enzyme activity and had no influence on dimer arrangement. The non-conserved V26 residue, used as a negative control, did not contribute to the enzyme quaternary structure or activity. Detailed biophysical characterization of the wild-type and mutant proteins indicates that the mutations do not considerably alter the secondary structure of the enzyme but they affect dimer assembly. In addition, mutating residues V69, F73 and V168 disrupted the binding of AtNUDT7 to the regulatory 14.3.3 protein. These are the first studies of the structure-function relationship of AtNUDT7, a Nudix hydrolase of important regulatory function.

7

Flow cytometric enumeration of CD34plus hematopoietic stem and progenitor cells in leukapheresis product and bone marrow for clinical transplantation: a comparison of three methods

39%

Gajkowska A., Oldak T., Jastrzewska M., Machaj E. K., Walewski J., Kraszewska E., Pojda Z.

Folia Histochemica et Cytobiologica

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2006

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tom 44

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nr 1

8

Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and gamma subunits of the signal transducing heterotrimeric G protein

33%

Olejnik K., Bucholc M., Anielska-Mazur A., Lipko A., Kujawa M., Modzelan M., Augustyn A., Kraszewska E.

Acta Biochimica Polonica

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2011

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tom 58

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nr 4

Arabidopsis thaliana AtNUDT7 Nudix pyrophosphatase hydrolyzes NADH and ADP-ribose in vitro and is an important factor in the cellular response to diverse biotic and abiotic stresses. Several studies have shown that loss-of-function Atnudt7 mutant plants display many profound phenotypes. However the molecular mechanism of AtNUDT7 function remains elusive. To gain a better understanding of this hydrolase cellular role, proteins interacting with AtNUDT7 were identified. Using AtNUDT7 as a bait in an in vitro binding assay of proteins derived from cultured Arabidopsis cell extracts we identified the regulatory protein RACK1A as an AtNUDT7-interactor. RACK1A-AtNUDT7 interaction was confirmed in a yeast two-hybrid assay and in a pull-down assay and in Bimolecular Fluorescence Complementation (BiFC) analysis of the proteins transiently expressed in Arabidopsis protoplasts. However, no influence of RACK1A on AtNUDT7 hydrolase catalytic activity was observed. In vitro interaction between RACK1A and the AGG1 and AGG2 gamma subunits of the signal transducing heterotrimeric G protein was also detected and confirmed in BiFC assays. Moreover, association between AtNUDT7 and both AGG1 and AGG2 subunits was observed in Arabidopsis protoplasts, although binding of these proteins could not be detected in vitro. Based on the observed interactions we conclude that the AtNUDT7 Nudix hydrolase forms complexes in vitro and in vivo with regulatory proteins involved in signal transduction. Moreover, we provide the initial evidence that both signal transducing gamma subunits bind the regulatory RACK1A protein.

9

Dendritic cell-based vaccination against tumor antigens for melanoma and lymphoma patients

20%

Markowicz S., Biernacka M., Switaj T., Lipkowski A. W., Misicka A., Nowecki Z., Polowniak-Pracka H., Ruka W., Rutkowski P., Sawadro-Rochowska M., Skurzak H., Kraszewska E., Zurawski Z., Rymkiewicz G., Borawska A., Federowicz I., Rozewska D., Szymczyk M., Jakubowska-Mucka A., Pojda Z., Walewski J.

Acta Biochimica Polonica

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2006

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tom 53

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nr Supplement 1

Ograniczanie wyników

The plant Nudix hydrolase family

A mechanism that cuuples DNA transposition to cell differentiation ( Hypothesis)

Zastosowanie metody "kruchych pokryć" do badania naprężeń w kopytach

Nudix hydrolase PA5176 is linked to Rhamnolipids production in Pseudomonas aeruginosa

Transient and stable transformation of wheat with DNA preparations delivered by a biolistic method

Mutational analysis of the AtNUDT7 Nudix hydrolase from Arabidopsis thaliana reveals residues required for protein quarternary structure formation and activity

Flow cytometric enumeration of CD34plus hematopoietic stem and progenitor cells in leukapheresis product and bone marrow for clinical transplantation: a comparison of three methods

Arabidopsis thaliana Nudix hydrolase AtNUDT7 forms complexes with the regulatory RACK1A protein and gamma subunits of the signal transducing heterotrimeric G protein

Dendritic cell-based vaccination against tumor antigens for melanoma and lymphoma patients