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BACKGROUND Ripening-associated softening is one of the important attributes that largely determines the shelf-life of mango ( Mangifera indica Linn.) fruits. To reveal the effect of pre-climacteric ethylene treatment on ripening-related softening of Alphonso mango, ethylene treatment was given to mature, raw Alphonso fruits. Changes in the pool of reducing and non-reducing sugars, enzymatic activity of three glycosidases: β- d-galactosidase, α- d-mannosidase and β- d-glucosidase and their relative transcript abundance were analysed for control and ethylene treated fruits during ripening. RESULTS Early activity of all the three glycosidases and accelerated accumulation of reducing and non-reducing sugars on ethylene treatment was evident. β- d-Galactosidase showed the highest activity among three glycosidases in control fruits and marked increase in activity upon ethylene treatment. This was confirmed by the histochemical assay of its activity in control and ethylene treated ripe fruits. Relative transcript abundance revealed high transcript levels of β- d-galactosidase in control fruits. Ethylene-treated fruits showed early and remarkable increase in the β- d-galactosidase transcripts while α- d-mannosidase transcript variants displayed early accumulation. CONCLUSION The findings suggest reduction in the shelf-life of Alphonso mango upon pre-climacteric ethylene treatment, a significant role of β- d-galactosidase and α- d-mannosidase in the ripening related softening of Alphonso fruits and transcriptional regulation of their expression by ethylene. © 2016 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

BACKGROUND Linseed is the richest agricultural source of α-linolenic acid ( ALA), an ω-3 fatty acid ( FA) that offers several nutritional benefits. In the present study, sequence characterization of six desaturase genes ( SAD1, SAD2, FAD2, FAD2-2, FAD3A and FAD3B) and 3D structure prediction of their proteins from ten Indian linseed varieties differing in ALA content were performed to determine whether the nucleotide and amino acid ( AA) sequence variants have any functional implications in differential accumulation of ALA or other FAs in linseed. RESULTS The SAD and FAD2 genes exhibited few sequence variations among the ten varieties, forming only one or two protein isoforms. In contrast, the FAD3A and FAD3B genes showed more sequence variations and three or four protein isoforms. Interestingly, the two high- ALA varieties NL260 and Padmini had the same FAD3B nucleotide and protein isoforms, which differed from all other varieties. Surprisingly, no AA changes altered the 3D structures of the desaturase proteins. CONCLUSION Several nucleotide and AA sequence variations in desaturase genes were observed; however, they did not alter the 3D structure of any desaturase protein and were not correlated with FA levels among the ten linseed varieties, which had different ALA contents. This suggests a complex regulatory process of biosynthesis of FAs in linseed. © 2016 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Molecular changes elicited by plants in response to fungal attack and how this affects plant-pathogen interaction, including susceptibility or resistance, remain elusive. We studied the dynamics in root metabolism during compatible and incompatible interactions between chickpea and Fusarium oxysporum f. sp. ciceri (Foc), using quantitative label-free proteomics and NMR-based metabolomics. Results demonstrated differential expression of proteins and metabolites upon Foc inoculations in the resistant plants compared with the susceptible ones. Additionally, expression analysis of candidate genes supported the proteomic and metabolic variations in the chickpea roots upon Foc inoculation. In particular, we found that the resistant plants revealed significant increase in the carbon and nitrogen metabolism; generation of reactive oxygen species ( ROS), lignification and phytoalexins. The levels of some of the pathogenesis-related proteins were significantly higher upon Foc inoculation in the resistant plant. Interestingly, results also exhibited the crucial role of altered Yang cycle, which contributed in different methylation reactions and unfolded protein response in the chickpea roots against Foc. Overall, the observed modulations in the metabolic flux as outcome of several orchestrated molecular events are determinant of plant's role in chickpea-Foc interactions. [ABSTRACT FROM AUTHOR]

Helicoverpa armigera is a key pest in many vital crops, which is mainly controlled by chemical strategies. To manage this pest is becoming challenging due to its ability and evolution of resistance against insecticides. Further, its subsequent spread on nonhost plant is remarkable in recent times. Hence, decoding resistance mechanism against phytochemicals and synthetic insecticides is a major challenge. The present work describes that the digestion, defense and immunity related enzymes are associated with chlorpyrifos resistance in H. armigera. Proteomic analysis of H. armigera gut tissue upon feeding on chlorpyrifos containing diet (CH) and artificial diet (AD) using nano-liquid chromatography-mass spectrometry identified upregulated 23-proteins in CH fed larvae. Database searches combined with gene ontology analysis revealed that the identified gut proteins engrossed in digestion, proteins crucial for immunity, adaptive responses to stress, and detoxification. Biochemical and quantitative real-time polymerase chain reaction analysis of candidate proteins indicated that insects were struggling to get nutrients and energy in presence of CH, while at the same time endeavoring to metabolize chlorpyrifos. Moreover, we proposed a potential processing pathway of chlorpyrifos in H. armigera gut by examining the metabolites using gas chromatography-mass spectrometry. H. armigera exhibit a range of intriguing behavioral, morphological adaptations and resistance to insecticides by regulating expression of proteins involved in digestion and detoxification mechanisms to cope up with chlorpyrifos. In these contexts, as gut is a rich repository of biological information; profound analysis of gut tissues can give clues of detoxification and resistance mechanism in insects. [ABSTRACT FROM AUTHOR]

With 3 figures Abstract Genetic analysis of F2 and backcross populations of an induced temperature-sensitive genic male sterility (TGMS) mutant source F 61 with normal pollen parents revealed that TGMS trait was controlled by a single recessive gene. Molecular tagging of TGMS trait was attempted using polymorphic randomly amplified polymorphic DNA (RAPD) and simple sequence repeats (SSR) markers through bulked segregant analysis. The RAPD primers UBC 345830, UBC 313927, microsatellites RM224 and RM21 produced putative markers, which differentiate parents and bulks from sterile parent and sterile bulks. The RAPD analysis of individual F2 plants with the primer UBC345830 showed perfect marker-phenotype cosegregation. The 830-bp RAPD fragment, which segregated with TGMS locus at a distance of 1.33 cM, was eluted and cloned, and sequence information was used for designing sequence-characterized amplified region (SCAR) primer, which cosegregated with TGMS locus at a distance of 0.8 cM. TGMS locus was mapped onto chromosome 11 using RM21 and RM224, flanking it at a distance of 4.3 and 3.0 cM, respectively. The DNA markers tightly linked to TGMS gene ( tms8) in F 61 can be cost effectively used for marker-assisted selection of TGMS trait. [ABSTRACT FROM AUTHOR]

All the protein sequences from SWISS-PROT database were analyzed for occurrence of single amino acid repeats, tandem oligo-peptide repeats, and periodically conserved amino acids. Single amino acid repeats of glutamine, serine, glutamic acid, glycine, and alanine seem to be tolerated to a considerable extent in many proteins. Tandem oligo-peptide repeats of different types with varying levels of conservation were detected in several proteins and found to be conspicuous, particularly in structural and cell surface proteins. It appears that repeated sequence patterns may be a mechanism that provides regular arrays of spatial and functional groups, useful for structural packing or for one to one interactions with target molecules. To facilitate further explorations, a database of Tandem Repeats in Protein Sequences (TRIPS) has been developed and is available at URL: http://www.ncl-india.org/trips. [ABSTRACT FROM PUBLISHER]

Examines the role of pearl millet cysteine protease inhibitor (CPI) in an anti-fungal and anti-feedent activities. Impact of enzyme-based tryptophan on protein; Determination of the trichloroacetic acid-soluble casein hydrolysis product; Analysis of the biochemical properties of CPI.