Capsulization of Weather Broadcasting System using Raspberry pi

Weather broadcasting plays an important role in human life, so the collection of information about the temporal dynamics of weather changes is very important. The fundamental aim of this project is to develop an embedded system and design a weather broadcast system which enables the broadcasting of weather parameters for different sector. Such a system contain pair of sensors like temperature, pressure and humidity, which is used to sense the atmospheric parameter. Block diagram consist of the Raspberry pi, DHT-22 and BMP-180 sensor which is used for analyze the atmospheric parameters. The data from the sensors are collected by the microcontroller and it stored in SD cardand LCD screen is used to display the result

NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain

The CCR4-NOT complex plays a crucial role in post-transcriptional mRNA regulation in eukaryotes. This complex catalyzes the removal of mRNA poly(A) tails, thereby repressing translation and committing an mRNA to degradation. The conserved core of the complex is assembled by the interaction of at least two modules: the NOT module, which minimally consists of NOT1, NOT2 and NOT3, and a catalytic module comprising two deadenylases, CCR4 and POP2/CAF1. Additional complex subunits include CAF40 and two newly identified human subunits, NOT10 and C2orf29. The role of the NOT10 and C2orf29 subunits and how they are integrated into the complex are unknown. Here, we show that the Drosophila melanogaster NOT10 and C2orf29 orthologs form a complex that interacts with the N-terminal domain of NOT1 through C2orf29. These interactions are conserved in human cells, indicating that NOT10 and C2orf29 define a conserved module of the CCR4-NOT complex. We further investigated the assembly of the D. melanogaster CCR4-NOT complex, and demonstrate that the conserved armadillo repeat domain of CAF40 interacts with a region of NOT1, comprising a domain of unknown function, DUF3819. Using tethering assays, we show that each subunit of the CCR4-NOT complex causes translational repression of an unadenylated mRNA reporter and deadenylation and degradation of a polyadenylated reporter. Therefore, the recruitment of a single subunit of the complex to an mRNA target induces the assembly of the complete CCR4-NOT complex, resulting in a similar regulatory outcome

Method Development, Validation and Stability Indicating Studies for Simultaneous Estimation of Anti-Hypertensive Drugs from Pharmaceutical Formulation by RP-HPLC

Objective: Method development, validation & stability indicating studies for simultaneous estimation of Anti-Hypertensive drugs, Benidepine (BEN) and Metoprolol (MET) from pharmaceutical formulation by RP-HPLC. Methods: For present work, reverse phase chromatography was selected as its suggested use for ionic and moderate to non-polar compounds. Reverse phase chromatography is simple, suitable, better regarding efficiency, stability, and reproducibility. C18 packed column, a 100 X 2.1mm. ID column of 5.0 μm particle packing, was selected for separation of BEN and MET. Different solvent systems were tried and optimized in combinations as mobile phase. BEN (4 μg/ml) and MET (50 μg/ml) in 15mM ammonium formate-Methanol (15:85 v/v) was developed as it was showing good peak shapes and a significant amount of resolution. The mobile phase was flowed at 1.2 ml/min with detection of BEN analytes at 236 nm and MET analytes at 225 nm respectively. Result: Method development was done. Specificity, linearity, accuracy, precision, robustness, limit of detection and limit of quantitation were used to accomplish validation. The method was found linear from 32.5 – 500 µg.ml-1 for both BEN and MET individually. The percentage recovery of BEN when placed for period of 12 hours was found to 100% in 0.1N/M NaOH at 60˚C and Thermal (60˚C); 12 % degradation in 0.1N/M HCl at 60˚C; Oxidation (3-6% H2O2) at room temperature whereas for MET was 100 % in 0.1N/M NaOH, 0.1N/M HCl at 60˚C, at thermal (60˚C) as well as oxidation by 3-6% H2O2 at room temperature.  Conclusion: Developed analytical method for the simultaneous estimation of Benidipine (BED) and Metoprolol (MET) in both bulk and tablet formulation has obliged the ICH guidelines including, tailing factor (T), separation factors (α), theoretical plates (N), capacity factor (k’), resolution (R) and RSD (%). The validated stress degradation studies under thermal, oxidative, alkali and acid ascertained few degradation products for Benidipine whereas the Metoprolol was unaffected with forced degradation studies. Keywords: Benidipine, Metoprolol, Reverse-Phase High Performance Liquid Chromatography, Stability indicating method

An exon junction complex-independent function of Barentsz in neuromuscular synapse growth.

The exon junction complex controls the translation, degradation, and localization of spliced mRNAs, and three of its core subunits also play a role in splicing. Here, we show that a fourth subunit, Barentsz, has distinct functions within and separate from the exon junction complex in Drosophila neuromuscular development. The distribution of mitochondria in larval muscles requires Barentsz as well as other exon junction complex subunits and is not rescued by a Barentsz transgene in which residues required for binding to the core subunit eIF4AIII are mutated. In contrast, interactions with the exon junction complex are not required for Barentsz to promote the growth of neuromuscular synapses. We find that the Activin ligand Dawdle shows reduced expression in barentsz mutants and acts downstream of Barentsz to control synapse growth. Both barentsz and dawdle are required in motor neurons, muscles, and glia for normal synapse growth, and exogenous Dawdle can rescue synapse growth in the absence of barentsz. These results identify a biological function for Barentsz that is independent of the exon junction complex

A DDX6-CNOT1 complex and W-binding pockets in CNOT9 reveal direct links between miRNA target recognition and silencing

CCR4-NOT is a major effector complex in miRNA-mediated gene silencing. It is recruited to miRNA targets through interactions with tryptophan (W)-containing motifs in TNRC6/GW182 proteins and is required for both translational repression and degradation of miRNA targets. Here, we elucidate the structural basis for the repressive activity of CCR4-NOT and its interaction with TNRC6/GW182s. We show that the conserved CNOT9 subunit attaches to a domain of unknown function (DUF3819) in the CNOT1 scaffold. The resulting complex provides binding sites for TNRC6/GW182, and its crystal structure reveals tandem W-binding pockets located in CNOT9. We further show that the CNOT1 MIF4G domain interacts with the C-terminal RecA domain of DDX6, a translational repressor and decapping activator. The crystal structure of this complex demonstrates striking similarity to the eIF4G-eIF4A complex. Together, our data provide the missing physical links in a molecular pathway that connects miRNA target recognition with translational repression, deadenylation, and decapping

A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin

Human (Hs) Roquin1 and Roquin2 are RNA-binding proteins that promote mRNA target degradation through the recruitment of the CCR4-NOT deadenylase complex and are implicated in the prevention of autoimmunity. Roquin1 recruits CCR4-NOT via a C-terminal region that is not conserved in Roquin2 or in invertebrate Roquin. Here we show that Roquin2 and Drosophila melanogaster (Dm) Roquin also interact with the CCR4-NOT complex through their C-terminal regions. The C-terminal region of Dm Roquin contains multiple motifs that mediate CCR4-NOT binding. One motif binds to the CAF40 subunit of the CCR4-NOT complex. The crystal structure of the Dm Roquin CAF40-binding motif (CBM) bound to CAF40 reveals that the CBM adopts an a-helical conformation upon binding to a conserved surface of CAF40. Thus, despite the lack of sequence conservation, the C-terminal regions of Roquin proteins act as an effector domain that represses the expression of mRNA targets via recruitment of the CCR4-NOT complex

GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression

The eIF4E homologous protein (4EHP) is thought to repress translation by competing with eIF4E for binding to the 5' cap structure of specific mRNAs to which it is recruited through interactions with various proteins, including the GRB10-interacting GYF (glycine-tyrosine-phenylalanine domain) proteins 1 and 2 (GIGYF1/2). Despite its similarity to eIF4E, 4EHP does not interact with eIF4G and therefore fails to initiate translation. In contrast to eIF4G, GIGYF1/2 bind selectively to 4EHP but not eIF4E. Here, we present crystal structures of the 4EHP-binding regions of GIGYF1 and GIGYF2 in complex with 4EHP, which reveal the molecular basis for the selectivity of the GIGYF1/2 proteins for 4EHP. Complementation assays in a GIGYF1/2-null cell line using structure-based mutants indicate that 4EHP requires interactions with GIGYF1/2 to down-regulate target mRNA expression. Our studies provide structural insights into the assembly of 4EHP-GIGYF1/2 repressor complexes and reveal that rather than merely facilitating 4EHP recruitment to transcripts, GIGYF1/2 proteins are required for repressive activity

Outbreak of Multidrug-resistant Pseudomonas Aeruginosa Endophthalmitis Due to Contaminated Trypan Blue Solution

Purpose: To report the investigation of an outbreak of multidrug-resistant (MDR) Pseudomonas aeruginosa endophthalmitis in 13 patients after Cataract surgery and to emphasize on the importance of clinical profile, risk factors, and treatment outcomes. Methods: This was a hospital-based, retrospective case study with 13 consecutive patients who had manual small-incision Cataract surgery with intraocular lens (IOL) implantation and developed acute postoperative Pseudomonas aeruginosa endophthalmitis. The anterior chamber taps, vitreous aspirates, and environmental surveillance specimens were inoculated for culturing. Antibiotic susceptibility testing was performed using the agar diffusion method. Pulsed-field gel electrophoresis (PFGE) was used to determine the relationship between bacterial isolates recovered from study patients and contaminated surveillance samples. Results: Pseudomonas aeruginosa was isolated from all 13 eyes with acute postoperative endophthalmitis and the trypan blue solutions used during surgery. Sensitivity tests revealed that all isolates had an identical resistance to multiple drugs and were only susceptible to imipenem. Genomic DNA typing of Pseudomonas aeruginosa isolates recovered from patients and trypan blue solutions showed an identical banding pattern on the PFGE. Despite the prompt use of intravitreal antibiotics and early vitrectomy with IOL explantation in some patients, the outcome was poor in about 50% of patients. Conclusion: Positive microbiology and genomic DNA typing results proved that the contaminated trypan blue solutions were the source of infection in this outbreak. Postoperative endophthalmitis caused by Pseudomonas aeruginosa is often associated with a poor visual prognosis despite prompt treatment with intravitreal antibiotics