Pigeonpea nutrition and its improvement

Pigeonpea (Cajanus cajan [L.] Millsp.), known by several vernacular and names such as red gram, tuar, Angola pea. yellow dhal and oil dhal, is one of the major grain legume crops of the tropics and sub-tropics. It is a crop of small holder dryland fmmers because it can grow well under subsistence level of agriculture and provides nutritive food, fodder, and fuel wood. It also improves soil by fixing atmospheric nitrogen. India by far is the largest pigeonpea producer it is consumed as decorticated split peas, popularly called as 'dhaL' In other countries, its consumption as whole dty and green vegetable is popular. Its foliage is used as fodder and milling by-products [onn an excellent feed for domestic animals. Pigeonpea seeds contain about 20-22% protein and appreciable amounts of essential amino.acids and minerals. DehuHing and boiling treatments of seeds get rid of the most antinutritional factors as tannins and enzyme inhibitors. Seed storage causes considerable losses in the quality of this legume. The seed protein of pigeonpea has been successfully enhanced by breeding from 20-22% to 28-30%. Such lines also agronomically performed well and have acceptable and color. The high-protein lines were found nutritionally superior to the cultivars because they would provide more quantities of utilizable protein and sulfur-containing amino acids

Host metabolic interaction and perspectives in phytoplasma research

Phytoplasmas are plant pathogenic bacteria that have large economic impacts on crops and landscape plants. Knowledge of their biology is limited also because they are still not easily cultured in media. It is still a mystery how phytoplasmas use the sugar-rich phloem sap and how they interact with the hosts. It is agriculturally important to identify the factors involved in their pathogenicity and to discover effective measures to control phytoplasma-associated diseases. The knowledge about host-pathogen interaction during the infection process can help to elucidate the processes leading to symptom expression. Transcriptomics studies paved the way for analysing the gene expression pattern in phytoplasma-infected plants and revealed the up-regulation of genes responsible for hormonal balance, transcription factors, and signalling. Recent studies have identified potential virulence factors that induce some of the typical phytoplasma disease symptoms and have started the annotation of their genomes having unique reductive evolution features. The novel manipulation tool represented by the potential of the synthetic biology can be helpful for its potential application in studying efficient management strategies to reduce the agricultural impact of the diseases associated with the phytoplasma presence

Structural determination of functional units of the nucleotide binding domain (NBD94) of the reticulocyte binding protein Py235 of Plasmodium yoelii.

Invasion of the red blood cells (RBC) by the merozoite of malaria parasites involves a large number of receptor ligand interactions. The reticulocyte binding protein homologue family (RH) plays an important role in erythrocyte recognition as well as virulence. Recently, it has been shown that members of RH in addition to receptor binding may also have a role as ATP/ADP sensor. A 94 kDa region named Nucleotide-Binding Domain 94 (NBD94) of Plasmodium yoelii YM, representative of the putative nucleotide binding region of RH, has been demonstrated to bind ATP and ADP selectively. Binding of ATP or ADP induced nucleotide-dependent structural changes in the C-terminal hinge-region of NBD94, and directly impacted on the RBC binding ability of RH.In order to find the smallest structural unit, able to bind nucleotides, and its coupling module, the hinge region, three truncated domains of NBD94 have been generated, termed NBD94(444-547), NBD94(566-663) and NBD94(674-793), respectively. Using fluorescence correlation spectroscopy NBD94(444-547) has been identified to form the smallest nucleotide binding segment, sensitive for ATP and ADP, which became inhibited by 4-Chloro-7-nitrobenzofurazan. The shape of NBD94(444-547) in solution was calculated from small-angle X-ray scattering data, revealing an elongated molecule, comprised of two globular domains, connected by a spiral segment of about 73.1 A in length. The high quality of the constructs, forming the hinge-region, NBD94(566-663) and NBD94(674-793) enabled to determine the first crystallographic and solution structure, respectively. The crystal structure of NBD94(566-663) consists of two helices with 97.8 A and 48.6 A in length, linked by a loop. By comparison, the low resolution structure of NBD94(674-793) in solution represents a chair-like shape with three architectural segments.These structures give the first insight into how nucleotide binding impacts on the overall structure of RH and demonstrates the potential use of this region as a novel drug target