SUMMARYThe glyoxalase system constitutes the major pathway for the detoxification of metabolically produced cytotoxin methylglyoxal (MG) into a non-toxic metabolite D-lactate. Glyoxalase I (GLY I) is an evolutionarily conserved metalloenzyme requiring divalent metal ions for its activity: Zn 2+ in the case of eukaryotes or Ni 2+ for enzymes of prokaryotic origin. Plant GLY I proteins are part of a multimember family; however, not much is known about their physiological function, structure and metal dependency. In this study, we report a unique GLY I (OsGLYI-11.2) from Oryza sativa (rice) that requires Ni 2+ for its activity. Its biochemical, structural and functional characterization revealed it to be a monomeric enzyme, possessing a single Ni 2+ coordination site despite containing two GLY I domains. The requirement of Ni 2+ as a cofactor by an enzyme involved in cellular detoxification suggests an essential role for this otherwise toxic heavy metal in the stress response. Intriguingly, the expression of OsGLYI-11.2 was found to be highly substrate inducible, suggesting an important mode of regulation for its cellular levels. Heterologous expression of OsGLYI-11.2 in Escherichia coli and model plant Nicotiana tabacum (tobacco) resulted in improved adaptation to various abiotic stresses caused by increased scavenging of MG, lower Na + /K + ratio and maintenance of reduced glutathione levels. Together, our results suggest interesting links between MG cellular levels, its detoxification by GLY I, and Ni 2+ -the heavy metal cofactor of OsGLYI-11.2, in relation to stress response and adaptation in plants.

We study the aggradation and incision of the Alaknanda River Valley during the late Pleistocene and Holocene. The morphostratigraphy in the river valley at Deoprayag shows the active riverbed, a cut terrace, and a fill terrace. The sedimentary fabric of the fill terrace comprises four lithofacies representing 1) riverbed accretion, 2) locally derived debris fan, 3) the deposits of waning floods and 4) palaeoflood records. The sedimentation style, coupled with geochemical analysis and Optically Stimulated Luminescence (OSL) dating, indicate that this terrace formed in a drier climate and the river valley aggraded in two phases during 21–18 ka and 13–9 ka. During these periods, sediment supply was relatively higher. Incision began after 10 ka in response to a strengthened monsoon and aided by increase of the tectonic gradient. The cut terrace formed at ~ 5 ka during a phase of stable climate and tectonic quiescence. The palaeoflood records suggest wetter climate 200–300 yr ago when the floods originated in the upper catchment of the Higher Himalaya and in the relatively drier climate ~ 1.2 ka when locally derived sediments from the Lesser Himalaya dominated flood deposits. Maximum and minimum limits of bedrock incision rate at Deoprayag are 2.3 mm/a and 1.4 mm/a.

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The cellular levels of methylglyoxal (MG), a toxic byproduct of glycolysis, rise under various abiotic stresses in plants. Detoxification of MG is primarily through the glyoxalase pathway. The first enzyme of the pathway, glyoxalase I (GLYI), is a cytosolic metalloenzyme requiring either Ni or Zn for its activity. Plants possess multiple GLYI genes, of which only some have been partially characterized; hence, the precise molecular mechanism, subcellular localization and physiological relevance of these diverse isoforms remain enigmatic. Here, we report the biochemical properties and physiological role of a putative chloroplast-localized GLYI enzyme, OsGLYI-8, from rice, which is strikingly different from all hitherto studied GLYI enzymes in terms of its intracellular localization, metal dependency and kinetics. In contrast to its predicted localization, OsGLYI-8 was found to localize in the nucleus along with its substrate, MG. Further, OsGLYI-8 does not show a strict requirement for metal ions for its activity, is functional as a dimer and exhibits unusual biphasic steady-state kinetics with a low-affinity and a high-affinity substrate-binding component. Loss of AtGLYI-2, the closest Arabidopsis ortholog of OsGLYI-8, results in severe germination defects in the presence of MG and growth retardation under salinity stress conditions. These defects were rescued upon complementation with AtGLYI-2 or OsGLYI-8. Our findings thus provide evidence for the presence of a GLYI enzyme and MG detoxification in the nucleus.

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This is a conventional kind of monitoring study. The objective of the study was to assess and monitor the physicochemical parameters in wastewater at inlet and outlet of sewage treatment plant (STP) and also to study the effectiveness of the STPs. The average concentration of parameters at inlet sampling site pH, electrical conductivity, total dissolved solids, are 7.16, 2,169 lS/cm, 766.06 mg/l, and major ions bicarbonate, nitrate, sulphate, phosphate, chloride, sodium, potassium, magnesium and calcium values 515. 88, 4.28, 82.85, 15.17, 7.01, 23.08, 29.34, 4.14 and 84.31 mg/l. While the average concentration of these parameters, after treatment shows following values 7.47, 2,161.43 (lS/cm), 695.81, 436.52, 1.25, 99.22, 12.69, 6.83, 23.18, 29.07, 4.40 and 82.65 mg/l, respectively. Further, to check the Na % and sodium absorption ratio at inlet and outlet which 27.89 %, 0.67 and 28.19 %, 0.68, respectively, for the suitability of the wastewater. Finally, the agglomerative hierarchical clustering techniques were used to study the similarity in the sewage treatment plants. The result suggests that there is considerable improvement in the wastewater quality after treatment except at the Pappankalan and Coronation Pillar, Timarpur.

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