Genomic, Transcriptomic, and Proteomic Analysis Provide Insights Into the Cold Adaptation Mechanism of the Obligate Psychrophilic Fungus Mrakia psychrophila
Author(s) -
Su Yao,
Xianzhi Jiang,
Wenping Wu,
Manman Wang,
Muhammad Imran Hamid,
Meichun Xiang,
Xingzhong Liu
Publication year - 2016
Publication title -
g3 genes genomes genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.468
H-Index - 66
ISSN - 2160-1836
DOI - 10.1534/g3.116.033308
Subject(s) - psychrophile , biology , unfolded protein response , endoplasmic reticulum , major facilitator superfamily , gene , biochemistry , transcriptome , codon usage bias , proteome , genetics , gene expression , genome , enzyme , mutant
Mrakia psychrophila is an obligate psychrophilic fungus. The cold adaptation mechanism of psychrophilic fungi remains unknown. Comparative genomics analysis indicated that M. psychrophila had a specific codon usage preference, especially for codons of Gly and Arg and its major facilitator superfamily (MFS) transporter gene family was expanded. Transcriptomic analysis revealed that genes involved in ribosome and energy metabolism were upregulated at 4°, while genes involved in unfolded protein binding, protein processing in the endoplasmic reticulum, proteasome, spliceosome, and mRNA surveillance were upregulated at 20°. In addition, genes related to unfolded protein binding were alternatively spliced. Consistent with other psychrophiles, desaturase and glycerol 3-phosphate dehydrogenase, which are involved in biosynthesis of unsaturated fatty acid and glycerol respectively, were upregulated at 4°. Cold adaptation of M. psychrophila is mediated by synthesizing unsaturated fatty acids to maintain membrane fluidity and accumulating glycerol as a cryoprotectant. The proteomic analysis indicated that the correlations between the dynamic patterns between transcript level changes and protein level changes for some pathways were positive at 4°, but negative at 20°. The death of M. psychrophila above 20° might be caused by an unfolded protein response.
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