No abstract

A significantly fast reaction condition for the exclusive preparation β-glycosyl thiol derivatives has been developed successfully. The reaction condition is one-step, fast, high yielding, highly stereoselective, and requires only benchtop chemicals. Further reaction of glycosyl thiol derivatives with Michael acceptors and alkylating agents furnished thioglycosides and (1,1)-thiolinked trehalose analogs.

Soil salinity can be a major constraint to pigeonpea (Cajanus cajan (L.) Millsp.) in the regions where it is predominantly grown. This study was conducted to assess the extent of genetic variation for salinity tolerance in the germplasm of pigeonpea and its wild relatives. Solution culture experiments in a greenhouse and controlled environment chamber were conducted to screen a range of cultivated pigeonpea genotypes for ability to germinate and grow up to 60 d under saline conditions. Several wild relatives of pigeonpea were screened for salinity response in a sand culture system in a greenhouse. Among cultivated pigeonpea genotypes, ICPL 227 was one of the most tolerant and HY 3C one of the most sensitive genotypes tested. None of the pigeonpea genotypes tested were able to survive beyond 30 d at 8 dS nr 1 or higher salinity levels. The extent of variation in salinity response among cultivated pigeonpea genotypes appeared too limited to warrant genetic enhancement of salinity tolerance. Among the wild relatives of pigeonpea, various species of Atylosia, Rynchosia, and Dunbaria showed a wide range of variation in their salinity tolerance (critical levels from 4 to 12 dS nr 1): A. albicans (W. & A.) Benth., and A. platycarpa could grow in a sand culture system at 12 dS nr 1 and Rynchosia albiflora could not tolerate salinity levels above 4 dS nr 1. These results suggest that using wild relatives for genetic improvement may increase salinity tolerance of pigeonpea.

Aggregation of proteins with the expansion of polyglutamine tracts in the brain underlies progressive genetic neurodegenerative diseases (NDs) like Huntington's disease and spinocerebellar ataxias (SCA). An insensitive cellular proteotoxic stress response to non-native protein oligomers is common in such conditions. Indeed, upregulation of heat shock factor 1 (HSF1) function and its target protein chaperone expression has shown promising results in animal models of NDs. Using an HSF1 sensitive cell based reporter screening, we have isolated azadiradione (AZD) from the methanolic extract of seeds of Azadirachta indica, a plant known for its multifarious medicinal properties. We show that AZD ameliorates toxicity due to protein aggregation in cell and fly models of polyglutamine expansion diseases to a great extent. All these effects are correlated with activation of HSF1 function and expression of its target protein chaperone genes. Notably, HSF1 activation by AZD is independent of cellular HSP90 or proteasome function. Furthermore, we show that AZD directly interacts with purified human HSF1 with high specificity, and facilitates binding of HSF1 to its recognition sequence with higher affinity. These unique findings qualify AZD as an ideal lead molecule for consideration for drug development against NDs that affect millions worldwide.

The 5'-most open reading frame of the c.4kb RNA-2 of Indian peanut clump furovirus (IPCV) encodes a protein of 208 amino acids. This protein is thought to be the coat protein of IPCV because its amino acid composition and M(r) closely resemble those reported for IPCV coat protein and because its amino acid sequence is 61% identical to that of the coat protein of peanut clump virus (PCV) from West Africa. The extent of the sequence identity between IPCV and PCV coat proteins confirms previous conclusions that the viruses are distinct rather than strains of one virus. The sequences of the coat proteins of IPCV and PCV were between 18% and 26% identical to those of other furoviruses and those of unrelated tobamoviruses and tobraviruses. In contrast, the coat protein sequences were 37% (IPCV) and 36% (PCV) identical to that of the coat protein of barley stripe mosaic hordeivirus (BSMV). This similarity between the coat proteins of viruses from different groups (= genera) is unusual but is consistent with previous reports of sequence relatedness in various genes between certain furoviruses and BSMV.