Nada Slakeski

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Two genes encode (1→3, 1→4)-β-glucan 4-glucanohydrolase (EC 3.2.1.73) isoenzymes in barley. A gene for isoenzyme El has been isolated from a barley genomic library and the nucleotide sequence of a 4643 by fragment determined. The gene is located on barley chromosome 5 while the gene for (1→3, 1→4)-β-glucanase isoenzyme EII is carried on chromosome 1. The(More)
Two genes encode (1-->3,1-->4)-beta-d-glucan 4-glucanohydrolase (EC 3.2.1.73) isoenzymes EI and EII in barley (Hordeum vulgare L.). Specific DNA probes have been used in Northern analyses to examine the developmental regulation of individual (1-->3,1-->4)-beta-glucanase genes in the aleurone and scutellum of germinated grain and in young leaves and young(More)
Porphyromonas gingivalis is an anaerobic, asaccharolytic Gram-negative rod associated with chronic periodontitis. We have undertaken a proteomic study of the outer membrane of P. gingivalis strain W50 using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteins were identified by reference to the pre-release genomic sequence of P.(More)
Porphyromonas gingivalis is an anaerobic microorganism that inhabits the oral cavity, where oxidative stress represents a constant challenge. A putative transcriptional regulator associated with oxidative stress, an oxyR homologue, is known from the P. gingivalis W83 genome sequence. We used microarrays to characterize the response of P. gingivalis to H2O2(More)
Porphyromonas gingivalis is an anaerobic, asaccharolytic, gram-negative bacterium that has essential requirements for both iron and protoporphyrin IX, which it preferentially obtains as heme. A combination of large-scale quantitative proteomic analysis using stable isotope labeling strategies and mass spectrometry, together with transcriptomic analysis(More)
Porphyromonas gingivalis produces outer membrane-attached proteins that include the virulence-associated proteinases RgpA and RgpB (Arg-gingipains) and Kgp (Lys-gingipain). We analyzed the P. gingivalis outer membrane proteome and identified numerous proteins with C-terminal domains similar in sequence to those of RgpB, RgpA, and Kgp, indicating that these(More)
Protein substrates of a novel secretion system of Porphyromonas gingivalis contain a conserved C-terminal domain (CTD) of ∼70-80 amino acid residues that is essential for their secretion and attachment to the cell surface. The CTD itself has not been detected in mature substrates, suggesting that it may be removed by a novel signal peptidase. More than 10(More)
Porphyromonas gingivalis extracellular arginine- and lysine-specific proteinases have been implicated as major virulence factors in the development of adult periodontitis. We have previously purified a 48-kDa lysine-specific cysteine proteinase, designated PrtK48, from a P. gingivalis W50 cell-associated multiprotein complex. PrtK48 was non-covalently(More)
Porphyromonas gingivalis is a Gram-negative, anaerobic bacterium associated with chronic periodontitis. A 2D electrophoretic analysis of the outer membrane of P. gingivalis W50 revealed a dominant train of spots at 40-41 kDa. The proteins in the train of spots were digested in-gel with trypsin and identified by MS. The train of spots represented two(More)
Treatment of young barley leaves with indole acetic acid (IAA) or gibberellic acid (GA3) results in a dramatic increase in levels of (1----3,1----4)-beta-glucanase isoenzyme EI transcripts. In young roots of comparable age, levels of isoenzyme EI mRNA are high; IAA inhibits expression while GA3 has no effect on mRNA levels. The addition of both abscisic(More)