Effect of mycorrhiza (Glomus mosseae) on morphological and biochemical properties of Ashwagandha (Withania somnifera) (L.) Dunal

Mycorrhizal inoculation in the plant causing increase in growth and production of phytochemicals is well reported, however little information is available related to the effect of mycorrhiza on morphological and biochemical properties of the medicinal plants like Ashwagandha. The present study is an attempt on diversity analysis in Withania somnifera with an aim to ascertain the nature and extent of genetic diversity present among different accessions in presence of mycorrhiza. The major biochemical constituents of Ashwaganda roots are with nolides which are well known for its medicinal properties. Mycorrhizal associations confer benefits like better nutrition acquisition, enhanced growth, defense enhancement and improved abiotic and biotic stress tolerance in plants. The present investigation was undertaken to assess genetic diversity among five different accessions of W. somnifera using morphological and biochemical markers and the effect of mycorrrhizal inoculation on these marker. The present study concluded that presence of mycorrhiza was effective on plant growth and phytochemical constituents more than non-treated plants. Amongst five selected germplasms IC 283662, JA 134, RAS 23, MPAS 6 and MWS 205 of W. somnifera, JA 134 showed best response in pretext of the selected morphological and biochemical features in presence of mycorrhiza

Genetic analysis of wild and cultivated germplasm of pigeonpea using random amplified polymorphic DNA (RAPD) and simple sequence repeats (SSR) markers

The reliability of the quantification of genetic diversity using only one type of marker has been questioned as compared to the combined use of different markers. To compare the efficiency of the use of single versus multiple markers, the genetic diversity was quantified among 12 diverse pigeonpea germplasm comprised of eight wild and four cultivated using both random amplified polymorphic DNA (RAPD) and simple sequence repeat (SSR) markers, and how well these two types of markers discriminated the diverse pigeonpea germplasm was evaluated. The pigeonpea germplasm including eight wild species and four cultivated varieties was subjected to 40 RAPD and 40 microsatellite primers. The level of polymorphism as revealed by RAPD primers produced a total of 517 DNA fragments and all were found to be polymorphic that is, 100% and in SSR analysis 101 fragments were produced that too showed 100% polymorphism. The high similarity index value revealed by RAPD was 0.931 between GT-100 and ICPL-87 whereas through SSR, it was 1.00 between GTH-1 and GT-100 as well as Rhyncosia rothi and Rhyncosia minima. The least similarity index value revealed by RAPD (R. rothi and GTH-1) and SSR (Rhyncosia bracteata and ICPL-87) were 0.07 and 0.133, respectively. Using RAPD marker, the calculated arithmetic mean heterozygosity and the marker index were 0.90 and 22.47, respectively. The R. bracteata and ICPL-87 were found distinct from rest of other cultivars by showing only 13% similarity. Average PIC value shown by RAPD and SSR primers were found to be 0.90 and 0.18, respectively.Keywords: Pigeonpea, random amplified polymorphic DNA (RAPD), simple sequence repeats (SSR) markers.African Journal of Biotechnology Vol. 12(40), pp. 5823-583

The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system

Lafora disease (LD), a progressive form of inherited epilepsy, is associated with widespread neurodegeneration and the formation of polyglucosan bodies in the neurons. Laforin, a protein phosphatase, and malin, an E3 ubiquitin ligase, are two of the proteins that are defective in LD. We have shown recently that laforin and malin (referred together as LD proteins) are recruited to aggresome upon proteasomal blockade, possibly to clear misfolded proteins through the ubiquitin–proteasome system (UPS). Here we test this possibility using a variety of cytotoxic misfolded proteins, including the expanded polyglutamine protein, as potential substrates. Laforin and malin, together with Hsp70 as a functional complex, suppress the cellular toxicity of misfolded proteins, and all the three members of this complex are required for this function. Laforin and malin interact with misfolded proteins and promote their degradation through the UPS. LD proteins are recruited to the polyglutamine aggregates and reduce the frequency of aggregate-positive cells. Taken together, our results suggest that the malin–laforin complex is a novel player in the neuronal response to misfolded proteins and could be potential therapeutic targets for neurodegenerative disorders associated with cytotoxic proteins

Identification of RAPD marker for the White Backed Plant Hopper (WBPH) resistant gene in rice

The experimental material consisted of two parents Gurjari (white backed plant hopper resistant) and Jaya (white backed plant hopper susceptible) and their F2 progeny. The purpose of the study was the identification of RAPD (Random Amplified Polymorphic DNA) marker for white backed plant hopper (WBPH) resistant gene. The RAPD analysis was done group wise as well as combined for the bulk segregant analysis (BSA). For the BSA, of the total 50 random primers surveyed, a single linked primer, OPA 08, was identified. This primer generated 8-bands, one of which, OPA08-7, was putatively linked to resistant gene as was evident by its presence in almost all the resistant bulks and vice-versa. This band had molecular weight equal to 1219.38 bp and was found in resistant parent, Gurjari, and in almost all the resistant bulks (the four susceptible bulks revealed absence of the same band) indicating the band OPA08-7 as a marker for WBPH resistance among the screened rice genotypes

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Proline repeats, in cis- and trans-positions, confer protection against the toxicity of misfolded proteins in a mammalian cellular model

A broad range of neurodegenerative disorders result from the cytotoxicity conferred by aberrantly folded mutant proteins. Intriguingly, the cytotoxicity and aggregation property of a few mutant proteins are known to be modulated by the flanking sequences. One of such modulators is the proline repeat tract. Using a mammalian cellular model, we show here that proline repeat tract, both in cis- and in trans-positions, ameliorate the cytotoxicity of wide range of misfolded proteins coded by synthetic constructs. We further show that the proline repeat tract could possibly confer protection against the cytotoxicity of misfolded proteins by altering their conformation at the time of their synthesis. Thus, our study elucidates the mechanism by which the proline repeat tract might ameliorate the toxicity of misfolded proteins, and opens up new therapeutic modalities for disorders caused by cytotoxic misfolded proteins

Optimisation of Feed Trough Angle and Separating Trough Angle for best grading efficiency of Zero energy Multi Fruit Grader

The Guava grader was converted into multiple fruit grader and tested on five levels of inclination angle of feed trough (18.06, 19.42, 20.82, 22.17 and 23.50°) and separating trough (11.83, 12.65, 13.45, 14.27 and 15.08°). Variation of grading efficiency with different separating trough angle at fixed feed trough angles was studied. Over all grading efficiency was 93 % for mosambi, 95.70 % for guava and 90 % for orange. Optimum feed trough angle was found as 20.82 degree and separating trough angle as 14.27° for guava and mosambi. For orange, the optimum feed trough and separating trough angles were found as 19.45 and13.40, respectively, at which the efficiency was found as 90 %. The fruit grader was modified as an adjustable fruit grader that can be adjusted to grade as low as 50 (mm.) to 80 (mm.) diameter fruits and as high as 100 (mm.) to 150 (mm.) diameter fruits. The capacity of modified multi-fruit grader was found as 1200 kg/hr for guava and mosambi and 1125 kg/hr for orange at optimum efficiency

Spatial positions of homopolymeric repeats in the human proteome and their effect on cellular toxicity

Proteins with homopolymeric repeat tracts are very common in the human proteome. Intriguingly, some but not all repeat tracts show length variation in the population and, in a few, the expansion of repeat tract beyond the normal length is associated with neurodegenerative and developmental disorders. In this study we have addressed questions such as why some amino acid residues are favored in longer repeat tracts and why repeat tracts show terminal bias. Using cell biological assays for repeat tracts fused to green fluorescent protein we show here that homopolymeric repeats that are beyond their naturally occurring length in the proteome are cytotoxic in nature. This toxicity is further modulated by the length of the peptide that bears the repeat and the spatial location of the repeat within the peptide. Thus, the cellular toxicity appears to be one of the selective processes that regulate the evolution of homopolymeric repeats in the proteome

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