Your browser doesn't support javascript.
loading
Endoplasmic reticulum-quality control pathway and endoplasmic reticulum-associated degradation mechanism regulate the N-glycoproteins and N-glycan structures in the diatom Phaeodactylum tricornutum.
Chen, Jichen; Du, Hong; Liu, Zidong; Li, Tangcheng; Du, Hua; Wang, Wanna; Aslam, Muhammad; Chen, Weizhou; Li, Ping; Luo, Haodong; Fang, Hao; Liu, Xiaojuan.
Afiliação
  • Chen J; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Du H; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Liu Z; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Li T; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Du H; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Wang W; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Aslam M; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Chen W; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Li P; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Luo H; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Fang H; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China.
  • Liu X; Institute of Marine Sciences, Guangdong Provincial Key Laboratory of Marine Biotechnology and STU-UNIVPM Joint Algal Research Center, College of Sciences, Shantou University, Shantou, Guangdong, China. liuxiaojuan@stu.edu.cn.
Microb Cell Fact ; 21(1): 219, 2022 Oct 20.
Article em En | MEDLINE | ID: mdl-36266689
ABSTRACT
Tunicamycin inhibits the first step of protein N-glycosylation modification. However, the physiological, transcriptomic, and N-glycomic effects of tunicamycin on important marine diatom Phaeodactylum tricornutum are still unknown. In this study, comprehensive approaches were used to study the effects of tunicamycin stress. The results showed that cell growth and photosynthesis were significantly inhibited in P. tricornutum under the tunicamycin stress. The soluble protein content was significantly decreased, while the soluble sugar and neutral lipid were dramatically increased to orchestrate the balance of carbon and nitrogen metabolisms. The stress of 0.3 µg ml-1 tunicamycin resulted in the differential expression of ERQC and ERAD related genes. The upregulation of genes involved in ERQC pathway, the activation of anti-oxidases and the differential expression of genes related with ERAD mechanism might be important for maintaining homeostasis in cell. The identification of N-glycans, especially complex-type N-glycan structures enriched the N-glycan database of diatom P. tricornutum and provided important information for studying the function of N-glycosylation modification on proteins. As a whole, our study proposed working models of ERQC and ERAD will provide a solid foundation for further in-depth study of the related mechanism and the diatom expression system.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Diatomáceas / Degradação Associada com o Retículo Endoplasmático Tipo de estudo: Risk_factors_studies Idioma: En Revista: Microb Cell Fact Assunto da revista: BIOTECNOLOGIA / MICROBIOLOGIA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Diatomáceas / Degradação Associada com o Retículo Endoplasmático Tipo de estudo: Risk_factors_studies Idioma: En Revista: Microb Cell Fact Assunto da revista: BIOTECNOLOGIA / MICROBIOLOGIA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: China