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Aims: The prospective study was conducted with the aim to evaluate the prevalence and risk factors of gestational diabetes mellitus in a tertiary care referral hospital in Kerala., Materials and Methods: A prospective observational study was conducted with the aim to study the prevalence, risk factors, complications, treatment pattern and cost analysis of GDM. The study was carried out in the Obstetrics & Gynecology dDepartment of Al Shifa hHospital located in northern Kerala., Results: Over an eight-month period, 201 patients who met the inclusion criteria were enrolled for study from which prevalence of GDM was estimated at 15.9%. The study revealed higher prevalence of risk factors and complications such as age >25 years, BMI >26kg/m(2), family history of DM, past history GDM, history of big baby, gestational hypertension, vaginal candidiasis, premature rupture of membranes and hyperbilirubinemia in GDM group as compared to non-GDM group. The study also demonstrated that modern life-style was a major influencing factor for development of diabetes in the study population., Conclusion: The study reveals the necessity of proper screening diagnosis and management of GDM in pregnant women by the clinicians so as to prevent the future burden of type 2 diabetes., (Copyright © 2015 Diabetes India. Published by Elsevier Ltd. All rights reserved.)

The YycFG two-component system is the only signal transduction system in Bacillus subtilis known to be essential for cell viability. This system is highly conserved in low-G+C gram-positive bacteria, regulating important processes such as cell wall homeostasis, cell membrane integrity, and cell division. Four other genes, yycHIJK, are organized within the same operon with yycF and yycG in B. subtilis. Recently, it was shown that the product of one of these genes, the YycH protein, regulated the activity of this signal transduction system, whereas no function could be assigned to the other genes. Results presented here show that YycI and YycH proteins interact to control the activity of the YycG kinase. Strains carrying individual in-frame deletion of the yycI and yycH coding sequences were constructed and showed identical phenotypes, namely a 10-fold-elevated expression of the YycF-dependent gene yocH, growth defects, as well as a cell wall defect. Cell wall and growth defects were a direct result of overregulation of the YycF regulon, since a strain overexpressing YycF showed phenotypes similar to those of yycH and yycI deletion strains. Both YycI and YycH proteins are localized outside the cytoplasm and attached to the membrane by an N-terminal transmembrane sequence. Bacterial two-hybrid data showed that the YycH, YycI, and the kinase YycG form a ternary complex. The data suggest that YycH and YycI control the activity of YycG in the periplasm and that this control is crucial in regulating important cellular processes.

YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

The Bacillus subtilis YycFG two-component signal transduction system is essential for cell viability, and the YycH protein is part of the regulatory circuit that controls its activity. The crystal structure of YycH was solved by two-wavelength selenium anomalous dispersion data, and was refined using 2.3 A data to an R-factor of 25.2%. The molecule is made up of three domains, and has a novel three-dimensional structure. The N-terminal domain features a calcium binding site and the central domain contains two conserved loop regions.

A random phosphopeptide probe (bio-pYZZZ) has been used for the isolation and identification of multiple SH2 domains from human cDNA-displaying phage libraries. In addition, on-phage analysis and quantification of binding affinities for these phage-displayed proteins has shown them to be functional domains, retaining the same characteristics as in their native state.