Trust in Automation: A Critical Review

Current era of time can be characterized by the use of sophisticated instruments in almost all walks of life. These gadgets are handling those functions which were previously done by humans. Transfers of functions have thrown light on new avenues of knowledge pursuit. New horizons are being probed in general and reliability of the automated machines in particular. Human operators develop a state of trust while working on these machines. This paper has deliberated on the different aspects on trust in automated systems with the issues pertaining to use, misuse and disuse of the automation. Automation has opened new doors for solution of long standing problems, but at same time has posed new challenges in human-machine interaction

Toxic Phanerogamic Plants of Manipur

Volume: 99Start Page: 378End Page: 38

Genes involved in degradation of para-nitrophenol are differentially arranged in form of non-contiguous gene clusters in Burkholderia sp. strain SJ98.

Biodegradation of para-Nitrophenol (PNP) proceeds via two distinct pathways, having 1,2,3-benzenetriol (BT) and hydroquinone (HQ) as their respective terminal aromatic intermediates. Genes involved in these pathways have already been studied in different PNP degrading bacteria. Burkholderia sp. strain SJ98 degrades PNP via both the pathways. Earlier, we have sequenced and analyzed a ~41 kb fragment from the genomic library of strain SJ98. This DNA fragment was found to harbor all the lower pathway genes; however, genes responsible for the initial transformation of PNP could not be identified within this fragment. Now, we have sequenced and annotated the whole genome of strain SJ98 and found two ORFs (viz., pnpA and pnpB) showing maximum identity at amino acid level with p-nitrophenol 4-monooxygenase (PnpM) and p-benzoquinone reductase (BqR). Unlike the other PNP gene clusters reported earlier in different bacteria, these two ORFs in SJ98 genome are physically separated from the other genes of PNP degradation pathway. In order to ascertain the identity of ORFs pnpA and pnpB, we have performed in-vitro assays using recombinant proteins heterologously expressed and purified to homogeneity. Purified PnpA was found to be a functional PnpM and transformed PNP into benzoquinone (BQ), while PnpB was found to be a functional BqR which catalyzed the transformation of BQ into hydroquinone (HQ). Noticeably, PnpM from strain SJ98 could also transform a number of PNP analogues. Based on the above observations, we propose that the genes for PNP degradation in strain SJ98 are arranged differentially in form of non-contiguous gene clusters. This is the first report for such arrangement for gene clusters involved in PNP degradation. Therefore, we propose that PNP degradation in strain SJ98 could be an important model system for further studies on differential evolution of PNP degradation functions

Phylogenetic tree of amino acid sequences (A) <i>p</i>-nitrophenol 4-monooxygenase (PnpM), Benzenetriol dioxygenase (BtD) from stain SJ98 was taken as outgroup for the phylogenetic tree for PNP monooxygenases and (B) p-benzoquinone reductase (BqR), nitrite reductase from <i>E. coli</i> was taken as an outgroup to create the phylogenetic tree for the benzoquinone reductases.

<p>Neighbor joining method was applied at the bootstrap value of 1000. Accession number of the proteins is written in parentheses.</p

Comparison of <i>p</i>-nitrophenol (PNP) degradation gene clusters from different bacterial strains, schematic representation of the ORFs and distance between the gene clusters when arranged together as shown in <i>pnpAB</i> and <i>pnpCDE1E2F</i>

<div><p>(A) schematic representation of distance between Contig 11 (NZ_AJHK02000011.1) and contigs 12 (NZ_AJHK02000012.1) (B) if contigs 12 and then contigs 11 placed in series together then distance between the gene clusters and (C) PNP degradation gene clusters found in the other PNP degrading bacteria <i>Pseudomonas</i> sp. NyZ402 (GU123925.1), <i>Pseudomonas putida</i> DLLE-4 (FJ376608), <i>Pseudomonas</i> sp. 1-7 (FJ821777) and <i>Pseudomonas</i> sp. WBC-3 (EF577044).</p> <p>Similar genes have been assigned by the same colors.</p></div

Effect of Planting Date on Growth and Yield of Potato (Solanum tuberosum L.) in Semi-arid Tropics of Central India

The present experiment was carried out at the Research Farm of ICAR-Central Potato Research Institute (Regional Station), Gwalior (M.P.) during the Rabi season of 2021-22 to study the influence of planting dates on performance of potato crop. Total seven different planting date as treatments viz., D1- 15/09/2021; D2- 30/09/2021; D3- 15/10/2021; D4- 30/10/2021 (Timely planting); D5- 14/11/2021; D6- 29/11/2021 and D7-14/12/2021 were tested in randomized block design (RBD) with four replications. The potato (cv. Kufri Mohan) was planted with a seed rate of 3.5 t ha-1 and with a spacing of 60 cm x 20 cm. The recommended dose of chemical fertilizers viz., 180:80:120 kg ha-1 N:P2O5:K2O, respectively was applied to the crop. The various growth and yield attributes and yield viz., plant height, number of stem plant-1, haulm yield, tuber yield, biological yield and harvest Index were recorded. The results revealed that the timely planting treatment recorded 18.6-69.0% and 13.1-52.5% higher yield than early and late planting, respectively. Thus, the timely planting of potato (D4) showed significant positive effect on growth and yield of potato crop whereas the early (D2 and D2) and late planting (D6 and D7) treatments showed poor growth and yield performance

Predicted positions for the activity of <i>pnpA</i> and <i>pnpB</i> in <i>p</i>-nitrophenol (PNP) degradation pathway of strain SJ98.

<p>Predicted positions for the activity of <i>pnpA</i> and <i>pnpB</i> in <i>p</i>-nitrophenol (PNP) degradation pathway of strain SJ98.</p

Enzyme assay of <i>p</i>-nitrophenol 4-monooxygenase (PnpM)

<p>(A) Spectrophotometric analysis PnpM activity as shown by decrease in spectral absorption at 420 and 340 nm corresponding to depletion of <i>p</i>-nitrophenol (PNP) and NADH in a time dependent manner. (<b>B</b>) Lack of PnpM activity in negative control sample (<b>C</b>) Enzymatic transformation of PNP to BQ was confirmed by HPLC analysis.</p