No abstract

Peptidylarginine deiminases (PADs), a group of post-translational enzymes, catalyze the conversion of proteinbound arginine residues to citrulline residues in a calcium ion-dependent manner and are widely distributed in various organs of vertebrates. Although the existence of four isoforms of PAD (types I, II, III, and IV) is reported in rodents, the relative functions of the isoforms with respect to their colocation in the tissues have yet to be explored. In this study, we cloned the full-length cDNA encoding mouse PAD type I by screening a uterine cDNA library and using the RACE method. This cDNA consists of an open reading frame of 1989 bases encoding 662 amino acids (73 823 Da), a 5 H -untranslated region of 127 bases and a 3 H -untranslated region of 1639 bases. Comparative reverse transcription-PCR and Northern-blot analyses detected PAD type I mRNA only in the epidermis and uterus. Administration of estrogen to adult ovariectomized mice increased the content of PAD type I mRNA in the uterus, providing evidence that its expression is under the control of the sex steroid hormone. We also cloned the full-length cDNAs of mouse PAD type III and type IV by the reverse transcription-PCR and RACE methods. The primary structure of PAD type III contains 664 amino acids (75 098 Da) deduced from the coding region of 1995 bases, and the primary structure of PAD type IV consists of 666 amino acids (74 475 Da) deduced from the coding region of 2001 bases. Comparison of the deduced amino acid sequences of all four isoforms of PAD showed about 50% identity with each other, the 3 H regions being highly homologous compared with the 5 H regions.

A family 2b carbohydrate-binding module from Streptomyces thermoviolaceus STX-II was fused at the carboxyl-terminus of XynB, a thermostable and single domain family 10 xylanase from Thermotoga maritima, to create a chimeric xylanase. The chimeric enzyme (XynB-CBM2b) was puri¢ed and characterized. It displayed a pH^activity pro¢le similar to that of XynB and was stable up to 90 ‡C. XynB-CBM2b bound to insoluble birchwood and oatspelt xylan. Whereas its hydrolytic activities toward insoluble xylan and p-nitrophenyl-L L-xylopyranoside were similar to those of XynB, its activity toward soluble xylan was moderately higher than that of XynB. ß

The gene (agu)

The effluents from textile industries without proper treatment contains a remarkable amount of synthetic dyes which are harmful to the environment and a big challenge globally to degrade it with a eco-friendly way. Conventional methods are extremely energy-consuming, non-effective and generate a toxic sludge impacting the environment. Several microorganisms can be utilized to treat these effluents. The research deals with five bacteria isolated from textile effluent and their consortium for the biodegradation ability of Novacron dyes. The isolates were identified through the Biolog™ identification system and molecular technique. Biodegradation was confirmed by measuring optical density (OD) optimizing conditions (pH 7.0, temperature 37 °C, 10 % inoculums and 100 mg/L dye) under static condition. The isolates started decolourization at 24 h whereas, the consortium started decolourization at 18 h and exhibited a maximum after 72 h. The presence of low molecular weight protein as metabolite supported the biodegradation and non hazardous to environment. This study revealed that these bacteria might have degradation potentials, and research results will help to set up dye removal eco-friendly methods to expose the dye effulents to environment in future.

Campylobacter jejuni is one of the most prevalent organisms associated with foodborne illness across the globe causing campylobacteriosis and gastritis. Many proteins of C. jejuni are still unidentified. The purpose of this study was to determine the structure and function of a non-annotated hypothetical protein (HP) from C. jejuni. A number of properties like physiochemical characteristics, 3D structure, and functional annotation of the HP (accession No. CAG2129885.1) were predicted using various bioinformatics tools followed by further validation and quality assessment. Moreover, the protein-protein interactions and active site were obtained from the STRING and CASTp server, respectively. The hypothesized protein possesses various characteristics including an acidic pH, thermal stability, water solubility, and cytoplasmic distribution. While alpha-helix and random coil structures are the most prominent structural components of this protein, most of it is formed of helices and coils. Along with expected quality, the 3D model has been found to be novel. This study has identified the potential role of the HP in 2-methylcitric acid cycle and propionate catabolism. Furthermore, protein-protein interactions revealed several significant functional partners. The in-silico characterization of this protein will assist to understand its molecular mechanism of action better. The methodology of this study would also serve as the basis for additional research into proteomic and genomic data for functional potential identification.

The gene (agu)

Sonneratia apetala (S. apetala) (Lythraceae) has been investigated for the isolation and characterization of antimicrobial compounds and evaluation of their biological activities. The chloroform extract of the stem bark and different partitionate of the chloroform extracts i.e. Petroleum ether soluble fraction (PESF), Ethyl acetate soluble fraction(EASF), Methanol soluble fraction(MSF) and aqueous soluble fractions (ASF) were subjected to different chromatographic techniques to isolate secondary metabolites. Successive chromatographic separation and purification yielded a total of two compounds identified and characterized as Taraxerone(1) and 5,8-dihydroxy- 6-methoxy-4,9-dioxo-1,3,4,9-tetrahydronaphthol[2,3-c]furan-1-yl acetate (2) by extensive proton NMR spectrum (1H-NMRspectrum) analysis. The different partitionate like PESF, EASF, MESF and ASF were subjected to screen their antimicrobial properties against some selected Gram positive and Gram negative bacteria and fungi, brine shrimp lethality and antioxidant activities. The maximum zone of inhibition of chloroform extract was found against Pseudomonas sp. (16mm). All fractions showed more activity against Gram negative bacteria then Gram positive bacteria. In the brine shrimp lethality bioassay, among all extracts, the petroleum ether and ethyl acetate soluble fraction showed significant lethality having the LC50 value of 7.72 μg/ml. The antioxidant activity was evaluated in terms of determination of free radical scavenging activity (DPPH assay). Among all the extracts of S. apetala the highest free radical scavenging activity showed by (Methanol soluble fraction) MESF with IC50 value 18.0 μg/ml. Bangladesh J Microbiol, Volume 38, Number 1, June 2021, pp 1-5