Karyotypic diversity and evolution of seven mahseer species (Cyprinidae) from India

Mahseer is a group of fish species that are well known as food and game fishes. The taxonomy of the mahseer species is confusing owing to the morphological variations and habitat adaptation. Detailed karyomorphological investigations have been carried out in seven species of mahseer, using karyotyping, Ag-NOR and fluorescent staining techniques. The basic diploid chromosome number (2n), in all mahseer species, was observed to be 100; however, the karyotype formula varied among the species, which were recorded as: 20m + 14sm + 22st + 44t (fundamental arm number, FN = 134) in Tor khudree ; 22m + 24sm + 24st + 30t (FN = 146) in Tor mussullah; 12m + 22sm + 14st + 52t (FN = 134) in Tor putitora ; 20m + 24sm + 24st + 32t (FN = 144) in Tor tor ; 20m + 30sm + 24st + 26t (FN = 150) in Tor chelynoides; 20m + 20sm + 20st + 40t (FN = 140) in Tor progeneius; and 20m + 18sm + 14st + 48t (FN = 138) in Neolissochilus hexagonolepis . Silver staining of the chromosomes revealed the presence of multiple nucleolar organizer regions (NOR) in these mahseer species. The highest number of NORs was observed in T. tor (four pairs of chromosomes), whereas the other six species possessed Ag-NOR signals on only two pairs of chromosomes. Although chromomycin A₃ (CMA₃) staining induced bright fluorescence signals on same Ag-NORs sites, with CMA₃, one additional signal was observed on the p arm of subtelocentric chromosomes in T. tor , T. chelynoides , T. progeneius and N. hexagonolepis , which may indicate the presence of inactive NOR in these species. The information on cytogenetic profile of these mahseer species is discussed in the light of cytotaxonomic implications and understanding the karyoevolution of these fish species.     

Light activation of NADP malic enzyme in leaves of maize: marginal increase in activity,but marked change in regulatory properties of enzyme

This article reports the characteristics of light activation of NADP-malic enzyme (NADP-ME, EC 1.1.1.40) in leaf discs of maize (Zea mays cv. VMH 404) for the first time. The leaf discs were illuminated in the presence of 2 mmol/L bicarbonate, as light activation increases in the presence of bicarbonate. Upon illumination, the Vmax of NADP-ME increased by about 30%. Although small, the increase was consistent and significant. The changes in regulatory properties of NADP-ME were quite pronounced. The extent of light activation was similar when substrate (malate) concentration was either 4 mmol/L (saturating) or 0.01 mmol/L (limiting). There was only a marginal change in the Km for malate, but there was marked change in the response of NADP-ME to activators or inhibitors. The Ki for pyruvate and oxalate increased by 100 and 67% respectively, while the Ka for the citrate and succinate increased by 36 and 32% respectively. These results suggest that the NADP-ME becomes less sensitive to feedback inhibition on illumination. The light-induced change seems to be due, at least partially, to the reduction of dithiols, as incubation of leaf extracts with DTE dampened light activation of NADP-ME. We conclude that the properties of NADP-ME do change on illumination. Although there was only a marginal increase in the activity of the enzyme on illumination of leaf discs, the changes in regulatory properties of NADP-ME were marked.     

<Superscript>1</Superscript>H, <Superscript>13</Superscript>C and <Superscript>15</Superscript>N NMR assignments of an unusual Ca<Superscript>2+</Superscript>-binding protein from <Emphasis Type="Italic">Entamoeba histolytica</Emphasis> in its apo form

We report almost complete sequence specific ¹H, ¹³C and ¹⁵N NMR assignments of an unusual Ca²⁺-binding protein from Entamoeba histolytica (EhCaBP6) in its apo form as a prelude to its structural and functional characterization.     

Growth and proline accumulation in mungbean seedlings as affected by sodium chloride

Mungbean (Vigna radiata L. Wilczek cv. Sujata and cv. K851) seedlings were grown in paper towelins in dark under 0, 0.5, 1, 2 and 3 % (m/v) NaCl salinity. Germination percentage, shoot and root length, fresh mass of both cultivars decreased with salinity. Total soluble saccharides and proline accumulated in the root and shoot of salt stressed seedlings. The proline accumulation in the root was four to five times higher than that of the shoot of NaCl treated etiolated mungbean seedlings.     

Crystal Structure of Calcium Binding Protein-5 from Entamoeba histolytica and Its Involvement in Initiation of Phagocytosis of Human Erythrocytes

Entamoeba histolytica is the etiological agent of human amoebic colitis and liver abscess, and causes a high level of morbidity and mortality worldwide, particularly in developing countries. There are a number of studies that have shown a crucial role for Ca²⁺ and its binding protein in amoebic biology. EhCaBP5 is one of the EF hand calcium-binding proteins of E. histolytica. We have determined the crystal structure of EhCaBP5 at 1.9 Å resolution in the Ca²⁺-bound state, which shows an unconventional mode of Ca²⁺ binding involving coordination to a closed yet canonical EF-hand motif. Structurally, EhCaBP5 is more similar to the essential light chain of myosin than to Calmodulin despite its somewhat greater sequence identity with Calmodulin. This structure-based analysis suggests that EhCaBP5 could be a light chain of myosin. Surface plasmon resonance studies confirmed this hypothesis, and in particular showed that EhCaBP5 interacts with the IQ motif of myosin 1B in calcium independent manner. It also appears from modelling of the EhCaBP5-IQ motif complex that EhCaBP5 undergoes a structural change in order to bind the IQ motif of myosin. This specific interaction was further confirmed by the observation that EhCaBP5 and myosin 1B are colocalized in E. histolytica during phagocytic cup formation. Immunoprecipitation of EhCaBP5 from total E. histolytica cellular extract also pulls out myosin 1B and this interaction was confirmed to be Ca²⁺ independent. Confocal imaging of E. histolytica showed that EhCaBP5 and myosin 1B are part of phagosomes. Overexpression of EhCaBP5 increases slight rate (∼20%) of phagosome formation, while suppression reduces the rate drastically (∼55%). Taken together, these experiments indicate that EhCaBP5 is likely to be the light chain of myosin 1B. Interestingly, EhCaBP5 is not present in the phagosome after its formation suggesting EhCaBP5 may be playing a regulatory role.