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Genetic diversity and population structure of the amylolytic yeast Saccharomycopsis fibuligera associated with Baijiu fermentation in China
Ju-Wei Wang , Pei-Jie Han , Da-Yong Han , Sen Zhou , Kuan Li , Peng-Yu He , Pan Zhen , Hui-Xin Yu , Zhen-Rong Liang , Xue-Wei Wang , Feng-Yan Bai
J. Microbiol. 2021;59(8):753-762.   Published online July 5, 2021
DOI: https://doi.org/10.1007/s12275-021-1115-7
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  • 14 Crossref
AbstractAbstract
The amylolytic yeast Saccharomycopsis fibuligera is a predominant species in starters and the early fermentation stage of Chinese liquor (Baijiu). However, the genetic diversity of the species remains largely unknown. Here we sequenced the genomes of 97 S. fibuligera strains from different Chinese Baijiu companies. The genetic diversity and population structure of the strains were analyzed based on 1,133 orthologous genes and the whole genome single nucleotide polymorphisms (SNPs). Four main lineages were recognized. One lineage contains 60 Chinese strains which are exclusively homozygous with relatively small genome sizes (18.55–18.72 Mb) and low sequence diversity. The strains clustered in the other three lineages are heterozygous with larger genomes (21.85–23.72 Mb) and higher sequence diversity. The genomes of the homozygous strains showed nearly 100% coverage with the genome of the reference strain KPH12 and the sub-genome A of the hybrid strain KJJ81 at the above 98% sequence identity level. The genomes of the heterozygous strains showed nearly 80% coverage with both the sub-genome A and the whole genome of KJJ81, suggesting that the Chinese heterozygous strains are also hybrids with nearly 20% genomes from an unidentified source. Eighty-three genes were found to show significant copy number variation between different lineages. However, remarkable lineage specific variations in glucoamylase and α-amylase activities and growth profiles in different carbon sources and under different environmental conditions were not observed, though strains exhibiting relatively high glucoamylase activity were mainly found from the homozygous lineage.

Citations

Citations to this article as recorded by  
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    Food Innovation and Advances.2024; 3(4): 426.     CrossRef
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    Ying Huang, Dong Li, Yu Mu, Zhiyu Zhu, Yuzhang Wu, Qi Qi, Yingchun Mu, Wei Su
    Food Research International.2024; 176: 113805.     CrossRef
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    Food Research International.2024; 188: 114497.     CrossRef
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    Qi Yu, Feiyan Mou, Junwen Xiao, Cheng Zhan, Liang Li, Xu Chang, Xiaoyuan Dong, Maobin Chen, Xinrui Wang, Mei Chen, Shangling Fang
    World Journal of Microbiology and Biotechnology.2024;[Epub]     CrossRef
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    Food Research International.2024; 194: 114882.     CrossRef
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    Foods.2023; 12(22): 4140.     CrossRef
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    Food Research International.2023; 163: 112184.     CrossRef
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    Foods.2023; 12(15): 2936.     CrossRef
  • Comparison of physicochemical characteristics and microbiome profiles of low-temperature Daqu with and without adding tartary buckwheat
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    Food Bioscience.2022; 49: 101931.     CrossRef
  • What Are the Main Factors That Affect the Flavor of Sauce-Aroma Baijiu
    Jiao Niu, Shiqi Yang, Yi Shen, Wei Cheng, Hehe Li, Jinyuan Sun, Mingquan Huang, Baoguo Sun
    Foods.2022; 11(21): 3534.     CrossRef
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Research Support, Non-U.S. Gov't
Functional Analysis of the Invariant Residue G791 of Escherichia coli 16S rRNA
Woo-Seok Song , Hong-Man Kim , Jae-Hong Kim , Se-Hoon Sim , Sang-Mi Ryou , Sanggoo Kim , Chang-Jun Cha , Philip R. Cunningham , Jeehyeon Bae , Kangseok Lee
J. Microbiol. 2007;45(5):418-421.
DOI: https://doi.org/2595 [pii]
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AbstractAbstract
The nucleotide at position 791(G791) of E. coli 16S rRNA was previously identified as an invariant residue for ribosomal function. In order to characterize the functional role of G791, base substitutions were introduced at this position, and mutant ribosomes were analyzed with regard to their protein synthesis ability, via the use of a specialized ribosome system. These ribosomal RNA mutations attenuated the ability of ribosomes to conduct protein synthesis by more than 65%. A transition mutation (G to A) exerted a moderate effect on ribosomal function, whereas a transversion mutation (G to C or U) resulted in a loss of protein synthesis ability of more than 90%. The sucrose gradient profiles of ribosomes and primer extension analysis showed that the loss of protein-synthesis ability of mutant ribosomes harboring a base substitution from G to U at position 791 stems partially from its inability to form 70S ribosomes. These findings show the involvement of the nucleotide at position 791 in the association of ribosomal subunits and protein synthesis steps after 70S formation, as well as the possibility of using 16S rRNA mutated at position 791 for the selection of second-site revertants in order to identify ligands that interact with G791 in protein synthesis.

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