Genome-Wide Investigation of BAM Gene Family in Annona atemoya: Evolution and Expression Network Profiles during Fruit Ripening.

ß-amylase proteins (BAM) are important to many aspects of physiological process such as starch degradation. However, little information was available about the BAM genes in Annona atemoya, an important tropical fruit. Seven BAM genes containing the conservative domain of glycoside hydrolase family 14 (PF01373) were identified with Annona atemoya genome, and these BAM genes can be divided into four groups. Subcellular localization analysis revealed that AaBAM3 and AaBAM9 were located in the chloroplast, and AaBAM1.2 was located in the cell membrane and the chloroplast. The AaBAMs belonging to Subfamily I contribute to starch degradation have the higher expression than those belonging to Subfamily II. The analysis of the expression showed that AaBAM3 may function in the whole fruit ripening process, and AaBAM1.2 may be important to starch degradation in other organs. Temperature and ethylene affect the expression of major AaBAM genes in Subfamily I during fruit ripening. These expressions and subcellular localization results indicating ß-amylase play an important role in starch degradation.

Post-crotonylation oxidation by a monooxygenase promotes acetyl-CoA synthetase degradation in Streptomyces roseosporus.

Protein post-translational modifications (PTMs) with various acyl groups play central roles in Streptomyces. But whether these acyl groups can be further modified, and the influences of these potential modifications on bacterial physiology have not been addressed. Here in Streptomyces roseosporus with rich crotonylation, a luciferase monooxygenase LimB is identified to elaborately regulate the crotonylation level, morphological development and antibiotic production by oxidation on the crotonyl groups of an acetyl-CoA synthetase Acs. This chemical modification on crotonylation leads to Acs degradation via the protease ClpP1/2 pathway and lowered intracellular crotonyl-CoA pool. Thus, we show that acyl groups after PTMs can be further modified, herein named post-PTM modification (PPM), and LimB is a PTM modifier to control the substrate protein turnover for cell development of Streptomyces. These findings expand our understanding of the complexity of chemical modifications on proteins for physiological regulation, and also suggest that PPM would be widespread.

Evaluation of two wild castor (Ricinus communis L.) accessions for cadmium tolerance in relation to antioxidant systems and lipid peroxidation.

The present study was conducted to assess the effect of toxicity of cadmium (Cd) on growth, tolerance index (TI), antioxidant activities, and malondialdehyde (MDA) content in two contrasting wild castor accessions (16-024 and S2-4) via hydroponic experiment (0 and 100 mg/L Cd). The results showed that Cd significantly reduced the growth rate, seedling height, root length, and shoot length of the castor accessions compared to the control, with the Cd effect being more severe in S2-4 than in 16-024. In addition, biomass response including the root and shoot fresh weight and root dry weight decreased in both accessions compared to the control. Compared to the control group, the shoot dry weight of accession S2-4 declined by 21.7%, whereas there was no change in 16-024, suggesting a level of tolerance in 16-024. Analysis of TI on all the growth parameters and biomass content revealed that accession 16-024 was highly tolerant to Cd stress than S2-4. The results further revealed that the expression of the antioxidant enzymes, viz., superoxide dismutase (SOD), catalase (CAT), non-enzymatic antioxidant, glutathione, and MDA content, was influenced by genotype. S2-4 exhibited a higher antioxidant activity (SOD, CAT) and lipid peroxidation activity than 16-024, indicative of oxidative damage from Cd stress.