Plant Development: Early Events in Lateral Root Initiation

SummaryHow are the lateral root founder cells specified in the pericycle to initiate lateral root development? An Aux/IAA28 signaling module activates transcription factor GATA23 to control founder cell identity

Assessment of biotransfer and bioaccumulation of cadmium, lead and zinc from fly ash amended soil in mustard-aphid-beetle food chain.

The present study investigates the extent of biotransfer and bioaccumulation of cadmium (Cd), lead (Pb) and zinc (Zn) from fly ash amended soil in mustard (Brassica juncea)-aphid (Lipaphis erysimi)-beetle (Coccinella septempunctata) food chain and its subsequent implications for the beetle. The soil was amended with fly ash at the rates of 0, 5, 10, 20 and 40% (w/w). Our results showed that the uptake of Cd, Pb and Zn from soil to mustard root increased with the increase in fly ash application rates, but their root to shoot translocation was relatively restricted. Increase in chlorophyll content and dry mass of mustard plant on treatments ≥20% even at elevated accumulation of Cd (1.67mgkg(-1)), Pb (18.25mgkg(-1)) and Zn (74.45mgkg(-1) dry weight) in its shoot showed relatively higher tolerance of selected mustard cultivar to heavy metal stress. The transfer coefficient (TC(1)) of Cd from mustard shoot to aphid was always >1, indicating that Cd biomagnified in aphids at second trophic level. But, there was no biomagnification of Cd in adult beetles at third trophic level. Zinc accumulation was 2.06 to 2.40 times more in aphids than their corresponding host shoots and 1.26-1.35 times more in adult beetles than their prey (aphids) on which they fed. Lead was only metal whose TC was 0.05) biomass and predation rate of predatory beetles indicated that all levels of soil amendments with fly ash did not have any lethal or sub-lethal effects on beetles

Evaluation of an Antimicrobial L-Amino Acid Oxidase and Peptide Derivatives from Bothropoides mattogrosensis Pitviper Venom

Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a multifaceted mixture of peptides, proteins and inorganic components. L-amino oxidase (LAO) is a multifunctional enzyme that is able to develop different activities including antibacterial activity. In this study a novel LAO from Bothrops mattogrosensis (BmLAO) was isolated and biochemically characterized. Partial enzyme sequence showed full identity to Bothrops pauloensis LAO. Moreover, LAO here isolated showed remarkable antibacterial activity against Gram-positive and -negative bacteria, clearly suggesting a secondary protective function. Otherwise, no cytotoxic activities against macrophages and erythrocytes were observed. Finally, some LAO fragments (BmLAO-f1, BmLAO-f2 and BmLAO-f3) were synthesized and further evaluated, also showing enhanced antimicrobial activity. Peptide fragments, which are the key residues involved in antimicrobial activity, were also structurally studied by using theoretical models. The fragments reported here may be promising candidates in the rational design of new antibiotics that could be used to control resistant microorganisms

d-Maurocalcine, a Pharmacologically Inert Efficient Cell-penetrating Peptide Analogue*

Maurocalcine has been the first demonstrated animal toxin acting as a cell-penetrating peptide. Although it possesses competitive advantages, its use as a cell-penetrating peptide (CPP) requires that analogues be developed that lack its characteristic pharmacological activity on ryanodine-sensitive calcium channels without affecting its cell-penetrating and vector efficiencies. Here, we present the synthesis, three-dimensional 1H NMR structure, and activity of d-maurocalcine. We demonstrate that it possesses all of the desired features for an excellent CPP: preserved structure, lack of pharmacological action, conserved vector properties, and absence of cell toxicity. This is the first report of a folded/oxidized animal toxin in its d-diastereomer conformation for use as a CPP. The protease resistance of this new peptide analogue, combined with its efficient cell penetration at concentrations devoid of cell toxicity, suggests that d-maurocalcine should be an excellent vector for in vivo applications