Типологія синтаксичних конструкцій в німецькій та українській мовах

Німецька та українська мови є односистемними мовами: обидві належать до індоєвропейської мовної сім’ї. Спільні корені та тривалий період ізольованого розвитку, вказують на те, що вказані мови мають характеристики подібності та відмінності в своій внутрішній будові. Німецька та українська належать до синтетичного типу флективних мов. Це означає, що граматичне значення слів у них виражається, здебільшого, за допомогою системи флексій і реалізується в межах одного графічного слова. Але флективна система німецької мови бідніша, ніж у слов’янських мовах.Немецкий и украинский языки являются односистемными языками: оба принадлежат к индоевропейской языковой семье. Общие корни и длительный период изолированного развития, указывают на то, что указанные языки имеют характеристики сходства и различия в своем внутреннем строении. Немецкий и украинский принадлежат к синтетическому типу флективных языков. Это означает, что грамматическое значение слов в них выражается, в основном, с помощью системы флексий и реализуется в пределах одного графического слова. Но флективная система немецкого языка беднее, чем в славянских языках.German and Ukrainian are single-system languages: both belong to the Indo-European language family. Common roots and a long period of isolated development, indicate that these languages ​​have characteristics of similarity and differences in their internal structure. German and Ukrainian belong to the synthetic type of inflectional languages. This means that the grammatical meaning of words in them is expressed, mainly, with the help of a system of inflexions and is realized within a single graphic word. But the inflectional system of the German language is poorer than in the Slavic languages

Selected spots for MS analysis.

<p>(<b>A</b>) Coloured circles indicate the position on Pro-Q Diamond-stained gels of the 13 protein spots picked for MS analysis. Red circles are associated to hyperphosphorylated proteins; blue circles are associated to hypophosphorylated proteins. Boxes show an enlargement of picked spots. (<b>B</b>) Fold change values for the 13 selected spots. All the spots were differentially stained in anti-TG2-treated cells with respect to control IgG-treated cells. <i>P<0.05</i> (Student’s t-test).</p

MS analysis and database searching of the 13 spots with differential phosphorylation level in samples from anti-TG2 treated cells and from control-IgG treated cells.

<p>Spot number, UniProt protein ID and accession code, protein name, Mascot score, theoretical protein mass and pI values, number of peptide matches, sequence coverage and emPAI values are listed for each protein.</p

Representative 2-D-maps of phosphorylated and total proteins from Caco-2 cells treated with anti-TG2/control antibodies.

<p>Total protein extracts (150 µg) were separated on linear IPG strips 7 cm, pH 4.0–7.0, followed by 10%-sodium dodecyl sulphate polyacrylamide gel electrophoresis. 2-D gels were stained with the phosphoprotein-specific reagent Pro-Q Diamond (<b>A</b>) and with the SyproRuby dye to detect total proteins (<b>B</b>). 2-D-maps are representative of three biological independent replicates.</p

Validation of differential phosphorylation levels by western blot analysis.

<p>Total protein extracts (150 µg) from Caco-2 cells treated with anti-TG2 antibodies or with control IgG were separated by 2-DE using linear IPG strips, pH 5.5–6.7 for EF1γ (<b>A</b>), pH 4.7–5.9 for HSP60 (<b>B</b>), pH 3.9–5.1 for TCTP (<b>C</b>). Specific proteins were identified by immunoblot analysis.</p

Additional file 2: Table S3. of Chloroplast proteome response to drought stress and recovery in tomato (Solanum lycopersicum L.)

Identification details for the proteins observed as differentially represented by 2D-DIGE. Reported are spot number, protein accession/description, MASCOT score, total and unique peptides detected, identification rank and unicity, experimental and theoretical peptide mass value, peptide charge state, peptide mass error, number of peptide missed cleavage(s), peptide score, peptide expectation value and sequence, including amino acid(s) modification. (XLSX 1109 kb

Additional file 1: Table S1. of Chloroplast proteome response to drought stress and recovery in tomato (Solanum lycopersicum L.)

Nucleotide sequence of primers used for qRT-PCR analyses. Figure S1. Representative 2D-DIGE showing the resolution of about 2600 protein spots from tomato chloroplasts in IEF using pH 3-10 NL 18 cm strips, followed by 12% T SDS-PAGE. Spot visualization was obtained with a Typhoon fluorescence scanner. Differentially represented spots further subjected to nLC-ESI-LIT-MS/MS analysis are highlighted. A Cy-2 labeled pooled sample mixture was used as an internal standard for quantitative measurements. Table S2. Listed are data referring to spot number, NCBI protein accession number, protein description, MASCOT score value, theoretical and experimental molecular mass and pI values, total and unique peptides detected, sequence coverage (%), EMPAI score value, fold change in drought stressed plants with respect to control, and fold change in recovered drought stressed plants with respect to well-watered control of the same age. In addition, data referring to protein spots not showing significant quantitative variations are reported in italics and are highlighted in green. Protein species showing either an incoherent quantitative trend or a constant trend among the experimental conditions are highlighted in blue. (PDF 2377 kb

Disclosing the Interaction of Carbonic Anhydrase IX with Cullin-Associated NEDD8-Dissociated Protein 1 by Molecular Modeling and Integrated Binding Measurements

Human Carbonic Anhydrase (hCA) IX is a membrane-associated member of the CA enzyme family, involved in solid tumor acidification. This enzyme is a marker of tumor hypoxia and a prognostic factor for several human cancers. In a recent paper, we showed that CA IX interacts with cullin-associated NEDD8-dissociated protein 1 (CAND1), a nuclear protein involved in gene transcription and assembly of SCF ubiquitin ligase complexes. A functional role for this interaction was also identified, since lower CA IX levels were observed in cells with decreased CAND1 expression <i>via</i> shRNA-mediated interference. In this paper, we describe the identification of the structural determinants responsible for the CA IX/CAND1 interaction by means of a multidisciplinary approach, consisting of binding assay measurements, molecular docking, and site-directed mutagenesis. These data open a novel scenario in the design of anticancer drugs targeting CA IX. Indeed, the knowledge of the structural determinants responsible for the CAND1/CA IX interaction provides the molecular basis to design molecules able to destabilize it. Due to the proposed function of CAND1 in stabilizing CA IX, these molecules could represent an efficient tool to lower the amount of CA IX in hypoxic cancer cells, thus limiting its action in survival and the metastatic spread of tumors

Characterization of Carbonic Anhydrase IX Interactome Reveals Proteins Assisting Its Nuclear Localization in Hypoxic Cells

Carbonic anhydrase IX (CA IX) is a transmembrane protein affecting pH regulation, cell migration/invasion, and survival in hypoxic tumors. Although the pathways related to CA IX have begun to emerge, molecular partners mediating its functions remain largely unknown. Here we characterize the CA IX interactome in hypoxic HEK-293 cells. Most of the identified CA IX-binding partners contain the HEAT/ARM repeat domain and belong to the nuclear transport machinery. We show that the interaction with two of these proteins, namely XPO1 exportin and TNPO1 importin, occurs via the C-terminal region of CA IX and increases with protein phosphorylation. We also demonstrate that nuclear CA IX is enriched in hypoxic cells and is present in renal cell carcinoma tissues. These data place CA IX among the cell-surface signal transducers undergoing nuclear translocation. Accordingly, CA IX interactome involves also CAND1, which participates in both gene transcription and assembly of SCF ubiquitin ligase complexes. It is noteworthy that down-regulation of CAND1 leads to decreased CA IX protein levels apparently via affecting its stability. Our findings provide the first evidence that CA IX interacts with proteins involved in nuclear/cytoplasmic transport, gene transcription, and protein stability, and suggest the existence of nuclear CA IX protein subpopulations with a potential intracellular function, distinct from the crucial CA IX role at the cell surface

Characterization of Carbonic Anhydrase IX Interactome Reveals Proteins Assisting Its Nuclear Localization in Hypoxic Cells

Carbonic anhydrase IX (CA IX) is a transmembrane protein affecting pH regulation, cell migration/invasion, and survival in hypoxic tumors. Although the pathways related to CA IX have begun to emerge, molecular partners mediating its functions remain largely unknown. Here we characterize the CA IX interactome in hypoxic HEK-293 cells. Most of the identified CA IX-binding partners contain the HEAT/ARM repeat domain and belong to the nuclear transport machinery. We show that the interaction with two of these proteins, namely XPO1 exportin and TNPO1 importin, occurs via the C-terminal region of CA IX and increases with protein phosphorylation. We also demonstrate that nuclear CA IX is enriched in hypoxic cells and is present in renal cell carcinoma tissues. These data place CA IX among the cell-surface signal transducers undergoing nuclear translocation. Accordingly, CA IX interactome involves also CAND1, which participates in both gene transcription and assembly of SCF ubiquitin ligase complexes. It is noteworthy that down-regulation of CAND1 leads to decreased CA IX protein levels apparently via affecting its stability. Our findings provide the first evidence that CA IX interacts with proteins involved in nuclear/cytoplasmic transport, gene transcription, and protein stability, and suggest the existence of nuclear CA IX protein subpopulations with a potential intracellular function, distinct from the crucial CA IX role at the cell surface