BackgroundDNA methylation plays important biological roles in plants and animals. To examine the rice genomic methylation landscape and assess its functional significance, we generated single-base resolution DNA methylome maps for Asian cultivated rice Oryza sativa ssp. japonica, indica and their wild relatives, Oryza rufipogon and Oryza nivara.ResultsThe overall methylation level of rice genomes is four times higher than that of Arabidopsis. Consistent with the results reported for Arabidopsis, methylation in promoters represses gene expression while gene-body methylation generally appears to be positively associated with gene expression. Interestingly, we discovered that methylation in gene transcriptional termination regions (TTRs) can significantly repress gene expression, and the effect is even stronger than that of promoter methylation. Through integrated analysis of genomic, DNA methylomic and transcriptomic differences between cultivated and wild rice, we found that primary DNA sequence divergence is the major determinant of methylational differences at the whole genome level, but DNA methylational difference alone can only account for limited gene expression variation between the cultivated and wild rice. Furthermore, we identified a number of genes with significant difference in methylation level between the wild and cultivated rice.ConclusionsThe single-base resolution methylomes of rice obtained in this study have not only broadened our understanding of the mechanism and function of DNA methylation in plant genomes, but also provided valuable data for future studies of rice epigenetics and the epigenetic differentiation between wild and cultivated rice.

No abstract

Scope: Excessive consumption of processed meat has been linked to an increasing risk of gut diseases. It is investigated how pork meat proteins affect colon homeostasis between normal and immune-compromised mice. Methods and results: Immune-deficient mice (Rag1 −/− ) and wild-type mice are fed a diet that contains 20% casein or protein isolated from cooked pork or dry-cured pork for 3 months. Rag1 −/− mice show greater variations in transcriptome responses and higher microbial diversity than wild-type mice after consumption of the pork meat protein diets. Intake of pork meat protein diets also increases body weight and induces colonic oxidative stress, low-grade inflammation, and gene expression involved in immune function, cell cycle, and migration. Key genes like Hmox1, Ppara, and Pparg are highly upregulated by pork meat protein. These changes are associated with decreased abundances of Blautia, Bifidobacterium, and Alistipes and increased abundances of Akkermansia muciniphila and Ruminococcaceae. Conclusion: Pork meat proteins affect colon health in both wild-type and Rag1 −/− mice by altering the microbiome profile under the complex interaction with adaptive immunity. The findings herein give a new insight into the understanding of meat intake, immunity, and gut health.

The adsorption onto other minerals of charged gold nanoparticles, carried by gas ascending from the Earth's interior, is an important component of their transport and deposition in surficial cover such as alluvial, aeolian, and glacial sediments. To simulate the adsorption of these particles, an experiment was conducted in which a flow of air that contained gold nanoparticles was passed upward through a sample of alluvium from the middlelower reaches of the Yangtze River. These experiments showed that gold nanoparticles are adsorbed on kaolinite, halloysite, goethite, and hematite in the alluvial cover. Both the gold nanoparticles and minerals (i.e., kaolinite, halloysite, goethite, and hematite) carry surface charges that provide them with excellent adsorption properties. This study showed that the specific mineral composition of surficial alluvial cover affects the concentration of gold nanoparticles in the ascending gas. This phenomenon may plausibly be used in exploration for concealed gold, copper-gold, and silver-gold deposits in areas of thick alluvial cover.

No abstract

BACKGROUND Heat treatment induces both structural and digestive change of meat protein. However, little has been revealed regarding the associations between structural changes and digested peptides of myofibrillar proteins. This work investigated the effects of heat treatment on the structures and in vitro digestibility of actomyosin, and the peptidomics of the digests were analyzed using liquid chromatography tandem mass spectrometry (LC–MS/MS). RESULTS Heat treatment resulted in unfolding and aggregation behavior of actomyosin according to the results of surface hydrophobicity and particle size. Formation of disulfide bonds and increase in carbonyl groups that occurred during heat treatment of actomyosin indicated the oxidation of specific residues. Unfolding behavior could elevate digestibility of actomyosin by exposing residues, based on the identification of peptides in digests of actomyosin using LC–MS/MS. However, the disulfide bond proved to reduce the action of digestive proteases, since the peptides number (increased from 56 to 86 in sample heated at 70 °C for 30 min) and peptides intensity in digests largely increased after the addition of dithiothreitol (DTT). Heating at higher temperature (100 °C) induced severer aggregation and oxidation, which resulted in lower digestibility of actomyosin than that heated at 70 °C by burying or damaging partial cleavage sites for digestive proteases. CONCLUSIONS This work highlights the huge influence of heat treatment on the multi‐scale structures of myofibrillar proteins, which largely changed the peptides composition in protein digests. © 2019 Society of Chemical Industry

No abstract

In this work, we investigated changes in protein structures in vacuum-packed pork during chill storage and its impact on the in vitro protein digestion. Longissimus dorsi muscles were vacuum packed and stored at 4 • C for 3 days. Samples were subjected to Raman spectroscopy, in vitro digestion and nano LC-MS/MS. The 3 d samples had lower α-helix content, but higher β-sheet, β-turn, and random coil contents than the 0 d samples (P < 0.05). SDS-PAGE revealed significant protein degradation in the 3 d samples and the differences in digested products across the storage time. Proteome analysis indicated that the 3 d samples had the higher susceptibility to digestion. Increasing protein digestibility was mainly attributed to the degradation of myofibrillar proteins. Thus, exposure of more enzymatic sites in loose protein structure during chill storage could increase protein degradation in meat.