Overexpressing <i>Pleurotus ostreatus rho1b</i> results in transcriptional upregulation of the putative cellulolytic enzyme‐encoding genes observed in <i>ccl1</i> disruptants
Overexpressing <i>Pleurotus ostreatus rho1b</i> results in transcriptional upregulation of the putative cellulolytic enzyme‐encoding genes observed in <i>ccl1</i> disruptants
复制标题
过度表达平菇 rho1b 会导致在 ccl1 破坏体中观察到的假定纤维素分解酶编码基因的转录上调
DOI:
10.1111/1462-2920.15786
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发表时间:
2021
影响因子:
5.1
通讯作者:
Honda Yoichi
中科院分区:
文献类型:
--
作者:
Okuda Nozomi;Nakazawa Takehito;Horii Masato;Wu Hongli;Kawauchi Moriyuki;Sakamoto Masahiro;Honda Yoichi
The transcriptional expression pattern of lignocellulolytic enzyme‐encoding genes in white‐rot fungi differs depending on the culture conditions. Recently, it was shown that 13 putative cellulolytic enzyme‐encoding genes were significantly upregulated in mostPleurotus ostreatusligninolysis‐deficient mutant strains on beech wood sawdust medium. However, the mechanisms by which this transcriptional shift is triggered remain unknown. In this study, we identified one mechanism. Our previous study implied that histone H3N‐dimethylation at lysine 4 level possibly affects the shift; therefore, we analysed the expression pattern in the disruptants ofP. ostreatus ccl1, which encodes a putative component of the COMPASS complex mediating the methylation. The results showed upregulation of 5 of the 13 cellulolytic enzyme‐encoding genes. We also found thatrho1b, encoding a putative GTPase regulating signal transduction pathways, was upregulated in theccl1disruptants and ligninolysis‐deficient strains. Upregulation of at least three of the five cellulolytic enzyme‐encoding genes was observed inrho1b‐overexpressing strains but not inccl1/rho1bdouble‐gene disruptants, during the 20‐day culture period. These results suggest that Rho1b may be involved in the upregulation of cellulolytic enzyme‐encoding genes observed in theccl1disruptants. Furthermore, we suggest that Mpk1b, a putativeAgaricomycetes‐specific mitogen‐activated protein kinase, functions downstream of Rho1b.