A922 Sequential measurement of 1 hour creatinine clearance (1-CRCL) in critically ill patients at risk of acute kidney injury (AKI)

Meeting abstrac

Oligo- and dsDNA-mediated genome editing using a tetA dual selection system in Escherichia coli

The ability to precisely and seamlessly modify a target genome is needed for metabolic engineering and synthetic biology techniques aimed at creating potent biosystems. Herein, we report on a promising method in Escherichia coli that relies on the insertion of an optimized tetA dual selection cassette followed by replacement of the same cassette with short, single-stranded DNA (oligos) or long, double-stranded DNA and the isolation of recombinant strains by negative selection using NiCl2. This method could be rapidly and successfully used for genome engineering, including deletions, insertions, replacements, and point mutations, without inactivation of the methyl-directed mismatch repair (MMR) system and plasmid cloning. The method we describe here facilitates positive genome-edited recombinants with selection efficiencies ranging from 57 to 92%. Using our method, we increased lycopene production (3.4-fold) by replacing the ribosome binding site (RBS) of the rate-limiting gene (dxs) in the 1-deoxy-D-xylulose-5-phosphate (DXP) biosynthesis pathway with a strong RBS. Thus, this method could be used to achieve scarless, proficient, and targeted genome editing for engineering E. coli strains

Structural Similarity and Functional Diversity in Proteins containing the Legume Lectin Fold

Knowledge of structural relationship in proteins is increasingly proving very useful for in silico characterizations and is also being exploited as a prelude to almost every investigation in functional and structural genomics. A through understanding of the crutial features of a fold becomes necessary to realise the full potential of such relationship

Structural Similarity and Functional Diversity in Proteins containing the Legume Lectin Fold

Knowledge of structural relationship in proteins is increasingly proving very useful for in silico characterizations and is also being exploited as a prelude to almost every investigation in functional and structural genomics. A through understanding of the crutial features of a fold becomes necessary to realise the full potential of such relationship

Morphoanatomical And Physico-Chemical Studies Of Annona Reticulata, A Common Substitute For Annona Squamosa

The leaves of Annona reticulate Linn. (Annonaceae), commonly known as Bullock’s heart, are frequently used as a substitute for Annona squamosa for the treatment of diabetes by various tribes in India. The leaves are also used for their powerful insecticidal activity, especially for destroying lice. Pharmacognostical study of Annona reticulate leaf samples were studied using of light, confocal microscopy, WHO recommended physico-chemical  determinations and authentic phytochemcial procedures. Morphologically the leaves were dorsi-ventral in nature and were similar in external appearance to that of Annona squamosa. Anatomically the leaf of Annona reticulata presented significant features of a dicotyledonous leaf viz., upper epidermis, cortex, midrib and the lower epidermis. The physico-chemical,morphological and histological parameters presented in this paper may be proposed as parameters to establish the authenticity of Annona reticulata leaf and will be useful to differentiate the drug from Annona squamosa

Crystal Structures of Mycobacterium tuberculosis RecA and its complex ADP-AIF-4: implications for decreased ATPase activity and molecular aggregation

Sequencing of the complete genome of Mycobacterium tuberculosis, combined with the rapidly increasing need to improve tuberculosis management through better drugs and vaccines, has initiated extensive research on several key proteins from the pathogen. RecA, a ubiquitous multifunctional protein, is a key component of the processes of homologous genetic recombination and DNA repair. Structural knowledge of MtRecA is imperative for a full understanding of both these activities and any ensuing application. The crystal structure of MtRecA, presented here, has six molecules in the unit cell forming a 61 helical filament with a deep groove capable of binding DNA. The observed weakening in the higher order aggregation of filaments into bundles may have implications for recombination in mycobacteria. The structure of the complex reveals the atomic interactions of ADP–AlF4, an ATP analogue, with the P-loop-containing binding pocket. The structures explain reduced levels of interactions of MtRecA with ATP, despite sharing the same fold, topology and high sequence similarity with EcRecA. The formation of a helical filament with a deep groove appears to be an inherent property of MtRecA. The histidine in loop L1 appears to be positioned appropriately for DNA interaction