scholarly journals Peer Review #1 of "Diversity of the gut microbiome in three grasshopper species using 16S rRNA and determination of cellulose digestibility (v0.2)"

2020 ◽  
Keyword(s):  
16S Rrna ◽  
Peer Review ◽  
Gut Microbiome ◽  
Grasshopper Species ◽  
Cellulose Digestibility

scholarly journals Diversity of the gut microbiome in three grasshopper species using 16S rRNA and determination of cellulose digestibility

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e10194
Author(s):  
Jian-Mei Wang ◽  
Jing Bai ◽  
Fang-Yuan Zheng ◽  
Yao Ling ◽  
Xiang Li ◽  
...  
Keyword(s):  
Gut Microbiome ◽  
Intestinal Tract ◽  
Intestinal Microflora ◽  
Bacterial Species ◽  
Correlation Coefficients ◽  
Utilization Efficiency ◽  
Grasshopper Species ◽  
The Future ◽  
Cellulose Digestibility ◽  
And Function

Background Grasshoppers are typical phytophagous pests, and they have large appetites with high utilization of plants fibers, the digestion of which may depend on the microorganisms in their intestines. Grasshoppers have the potential to be utilized in bioreactors, which could improve straw utilization efficiency in the future. In this study, we describe the gut microbiome in three species of grasshoppers, Oedaleus decorus asiaticus, Aiolopus tamulus and Shirakiacris shirakii, by constructing a 16S rDNA gene library and analyzed the digestibility of cellulose and hemicellulose in the grasshoppers by using moss black phenol colorimetry and anthrone colorimetry. Results There were 509,436 bacterial OTUs (Operational Taxonomic Units) detected in the guts of all the grasshoppers sampled. Among them, Proteobacteria and Firmicutes were the most common, Aiolopus tamulus had the highest bacterial diversity, and Shirakiacris shirakii had the highest bacterial species richness. The intestinal microflora structure varied between the different species of grasshopper, with Aiolopus tamulus and Shirakiacris shirakii being the most similar. Meanwhile, the time at which grasshopper specimens were collected also led to changes in the intestinal microflora structure in the same species of grasshoppers. Klebsiella may form the core elements of the microflora in the grasshopper intestinal tract. The digestibility of cellulose/hemicellulose among the three species grasshoppers varied (38.01/24.99%, 43.95/17.21% and 44.12/47.62%). LEfSe analysis and Spearman correlation coefficients showed that the hemicellulosic digestibility of Shirakiacris shirakii was significantly higher than that of the other two species of grasshopper, which may be related to the presence of Pseudomonas, Stenotrophomonas, Glutamicibacter, Corynebacterium, and Brachybacterium in Shirakiacris shirakii intestinal tract. Conclusion The intestinal microbial communities of the three grasshoppers species are similar on phylum level, but the dominant genera of different species grasshoppers are different. The cellulose digestibility of the three species of grasshoppers is relatively high, which may be correlated with the presence of some gut microbiome. Increasing the understanding of the structure and function of the grasshopper intestinal microflora will facilitate further research and the utilization of intestinal microorganisms in the future.

Imaging of ribosomal RNA-protein interactions by dark-field STEM

1989 ◽  
Vol 47 ◽  
pp. 250-251
Author(s):  
M. Boublik ◽  
V. Mandiyan ◽  
S. Tumminia ◽  
J.F. Hainfeld ◽  
J.S. Wall
Keyword(s):  
Nucleic Acid ◽  
16S Rrna ◽  
Dark Field ◽  
Radius Of Gyration ◽  
Central Domain ◽  
The Core ◽  
16S Rna ◽  
30S Subunit ◽  
Core Particles

Success in protein-free deposition of native nucleic acid molecules from solutions of selected ionic conditions prompted attempts for high resolution imaging of nucleic acid interactions with proteins, not attainable by conventional EM. Since the nucleic acid molecules can be visualized in the dark-field STEM mode without contrasting by heavy atoms, the established linearity between scattering cross-section and molecular weight can be applied to the determination of their molecular mass (M) linear density (M/L), mass distribution and radius of gyration (RG). Determination of these parameters promotes electron microscopic imaging of biological macromolecules by STEM to a quantitative analytical level. This technique is applied to study the mechanism of 16S rRNA folding during the assembly process of the 30S ribosomal subunit of E. coli. The sequential addition of protein S4 which binds to the 5'end of the 16S rRNA and S8 and S15 which bind to the central domain of the molecule leads to a corresponding increase of mass and increased coiling of the 16S rRNA in the core particles. This increased compactness is evident from the decrease in RG values from 114Å to 91Å (in “ribosomal” buffer consisting of 10 mM Hepes pH 7.6, 60 mM KCl, 2 m Mg(OAc)2, 1 mM DTT). The binding of S20, S17 and S7 which interact with the 5'domain, the central domain and the 3'domain, respectively, continues the trend of mass increase. However, the RG values of the core particles exhibit a reverse trend, an increase to 108Å. In addition, the binding of S7 leads to the formation of a globular mass cluster with a diameter of about 115Å and a mass of ∽300 kDa. The rest of the mass, about 330 kDa, remains loosely coiled giving the particle a “medusa-like” appearance. These results provide direct evidence that 16S RNA undergoes significant structural reorganization during the 30S subunit assembly and show that its interactions with the six primary binding proteins are not sufficient for 16S rRNA coiling into particles resembling the native 30S subunit, contrary to what has been reported in the literature.

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