• 제목/요약/키워드: post translational modification

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New Insights into the Protein Turnover Regulation in Ethylene Biosynthesis

  • Yoon, Gyeong Mee
    • Molecules and Cells
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    • 제38권7호
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    • pp.597-603
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    • 2015
  • Biosynthesis of the phytohormone ethylene is under tight regulation to satisfy the need for appropriate levels of ethylene in plants in response to exogenous and endogenous stimuli. The enzyme 1-aminocyclopropane-1-carboxylic acid synthase (ACS), which catalyzes the rate-limiting step of ethylene biosynthesis, plays a central role to regulate ethylene production through changes in ACS gene expression levels and the activity of the enzyme. Together with molecular genetic studies suggesting the roles of post-translational modification of the ACS, newly emerging evidence strongly suggests that the regulation of ACS protein stability is an alternative mechanism that controls ethylene production, in addition to the transcriptional regulation of ACS genes. In this review, recent new insight into the regulation of ACS protein turnover is highlighted, with a special focus on the roles of phosphorylation, ubiquitination, and novel components that regulate the turnover of ACS proteins. The prospect of cross-talk between ethylene biosynthesis and other signaling pathways to control turnover of the ACS protein is also considered.

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

  • Im, Eunju;Chung, Kwang Chul
    • BMB Reports
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    • 제49권9호
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    • pp.459-473
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    • 2016
  • Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of NDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs.

동물세포 배양반응기

  • 오덕재
    • 미생물과산업
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    • 제20권2호
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    • pp.33-40
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    • 1994
  • 미생물에 대한 유전자 재조합법 등의 개발로 동물세포에서만 합성되던 단백질들을 미생물을 통하여 생산하는 기술이 확립되어 있으나, 동물 세포내에서만 정확하게 실행되어지는 단백질 분자의 folding과 post-translational modification 등이 미생물에서는 불완전하게 이루어져 활성을 잃게 되는 단점이 있고, pyrogen과 같이 미생물로부터 유래한 endotoxin이 생산물에 섞여 있을수도 있으며, 미생물로부터 생산되는 각종 단백질로부터 원하는 유용 단백질을 분리하기 어려운것 등, 현실적으로 많은 어려움을 가지고 있기 때문에 미생물을 이용하기보다 동물 세포 배양을 통하여 위와 같은 제재들을 생산하려 하고 있다. 유전자 재조합 기술은, 현재 미생물뿐만 아니라, 동,식물 세포에 대하여도 적용되어 있어서 각종 유용생산물을 동,식물세포의 유전자 조작을 통해 얻을 수 있는 단계에 와 있으며, 이는 유전자 치료(gene therapy)와 같은 의료분야에까지 확장될 수 있게 되었다. 표 2에서는 동물 세포를 배양할 때와 미생물을 이용할 때의 각각의 특징을 보여주고 있다.

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Absidia zychae가 생산하는 Serine-type Carboxypeptidase의 다양성 (Multiple Forms of Serine-type Carboxypeptidase Produced by Absidia zychae)

  • 이병로;안병용
    • KSBB Journal
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    • 제8권4호
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    • pp.405-408
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    • 1993
  • Absidia zychae NRIC 1199 produced two forms of carboxypeptidase(CPZ-1 and CPZ-2) which were distinguished in their isoelectric points but had almost identical properties(1). The amino acid sequences for the N-terminal of both enzymes were the same (Tyr-Thr-Ser-Pro-Lys-Leu-Xaa-Asp-Pro-Asp-Val) and any significant difference was not observed between amino acid compositions of the two enzymes. The ouchterlony double diffusion technique using antibody raised against the CPZ-2 protein demonstrated a good cross-reaction between CPZ-1 and CPZ-2 Genomic Southern analysis showed only one gene encoding CPZ in the genome of Absidia zychae. However, a significant difference between two enzymes was observed on peptide map using Staphylococcus aureus V8 protease, distinguishable only one band, indicating that multiple forms of CPZ are caused by post-translational modification, such as deamidation.

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Purification and Structural Studies on Human Pro-ghrelin

  • Yun, Ji-Hye;Lee, Jee-Won;Lee, Weon-Tae
    • 한국자기공명학회논문지
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    • 제12권1호
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    • pp.40-50
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    • 2008
  • Ghrelin is a unique peptide hormone that releases growth factor and it stimulates appetite. It comes from pre pro-ghrelin by the post translational modification process and its innate functions are known as food up-take and the growth hormone regulation. Therefore, the structural information of ghrelin precursor is of importance in understanding it function. From our results, we found that the solution structure of ghrelin is mostly random coil conformation at neutral pH value and the structural population changes with pH environments. Data from circular dichroism in different TFE concentrations revealed that the secondary structure changes from random coil to a-helix and the isodichroic point is observed at 202nm, implying that two equilibrium states exist between random coil and helical structure.

Peroxiredoxins and the Regulation of Cell Death

  • Hampton, Mark B.;O'Connor, Karina M.
    • Molecules and Cells
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    • 제39권1호
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    • pp.72-76
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    • 2016
  • Cell death pathways such as apoptosis can be activated in response to oxidative stress, enabling the disposal of damaged cells. In contrast, controlled intracellular redox events are proposed to be a significant event during apoptosis signaling, regardless of the initiating stimulus. In this scenario oxidants act as second messengers, mediating the post-translational modification of specific regulatory proteins. The exact mechanism of this signaling is unclear, but increased understanding offers the potential to promote or inhibit apoptosis through modulating the redox environment of cells. Peroxiredoxins are thiol peroxidases that remove hydroperoxides, and are also emerging as important players in cellular redox signaling. This review discusses the potential role of peroxiredoxins in the regulation of apoptosis, and also their ability to act as biomarkers of redox changes during the initiation and progression of cell death.

Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin

  • Danbi Yoon;Ju Heun Moon;Anna Cho;Hyejoon Boo;Jeong Seok Cha;Yoonji Lee;Jiho Yoo
    • Molecules and Cells
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    • 제46권6호
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    • pp.337-344
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    • 2023
  • N-glycosylation, a common post-translational modification, is widely acknowledged to have a significant effect on protein stability and folding. N-glycosylation is a complex process that occurs in the endoplasmic reticulum (ER) and requires the participation of multiple enzymes. GlcNAc-1-P-transferase (GPT) is essential for initiating N-glycosylation in the ER. Tunicamycin is a natural product that inhibits N-glycosylation and produces ER stress, and thus it is utilized in research. The molecular mechanism by which GPT triggers N-glycosylation is discussed in this review based on the GPT structure. Based on the structure of the GPT-tunicamycin complex, we also discuss how tunicamycin reduces GPT activity, which prevents N-glycosylation. This review will be highly useful for understanding the role of GPT in the N-glycosylation of proteins, as well as presents a potential for considering tunicamycin as an antibiotic treatment.

Characterization of a novel Cotesia vestalis polydnavirus (CvBV) gene containing a ser-rich motif expressed in Plutella xylostella larvae

  • Shi, Min;Chen, Ya-Feng;Huang, Fang;Zhou, Xue-Ping;Chen, Xue-Xin
    • BMB Reports
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    • 제41권8호
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    • pp.587-592
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    • 2008
  • Cotesia vestalis is an endoparasitoid of Plutella xylostella larvae and injects a polydnavirus (CvBV) into its host during oviposition. In this report we characterize the gene, CvBV3307, and its products. CvBV3307 is located on segment S33 of the CvBV genome, is 517 bp, and encodes a putative protein of 122 amino acids, including a serine-rich region. The expression pattern of CvBV3307 in parasitized larvae and the subcellular localization of CvBV3307 only in granulocytes indicated that it might be involved in early protection of parasitoid eggs from host cellular encapsulation and in manipulating the hormone titer and developmental rhythm of host larvae. Western blot analysis showed that the size of the immunoreactive protein (about 55 kDa) in parasitized hosts at 48 hours post parasitization (h p.p.) is much larger than the predicted molecular weight of 13.6 kDa, which suggests that CvBV3307 undergoes extensive post-translational modification in hosts.

식물의 물부족 스트레스 신호 전달 네트워크에 대한 이해 (Understanding of Drought Stress Signaling Network in Plants)

  • 이재훈
    • 생명과학회지
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    • 제28권3호
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    • pp.376-387
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    • 2018
  • 식물이 접하는 다양한 환경 스트레스(고온, 저온, 냉해, 고염, 가뭄 등) 중에서 물부족(가뭄) 스트레스는 식물의 생장 및 생산성을 저해하는 가장 주요한 요인으로 보고되어 왔다. 그러므로, 물부족 스트레스에 대한 식물의 반응 기작을 명확히 이해하는 것은 물부족 스트레스 저항성이 증가된 유용 작물 개발에 적용될 수 있을 것으로 기대되며, 그 결과 작물 재배 가능 지역의 확대에 기여할 수 있을 것으로 생각된다. 식물의 물부족 스트레스 신호 과정은 크게 식물 호르몬인 앱시스산 의존적인 과정과 비의존적인 과정으로 분류되며, 각각 AREB/ABF, DREB2 전사 조절 인자가 주요한 전사 조절 인자로 참여하여 하위 단계 반응 유전자의 발현 조절에 참여한다. 이러한 AREB/ABF, DREB2 의존적인 regulon에 대한 연구를 통해 물부족 스트레스 신호 과정 중 전사 수준의 조절에 대한 규명이 활발히 이루어지고 있다. 해당 신호 과정에는 전사 수준의 조절뿐만 아니라 인산화, 유비퀴틴화와 같은 번역 후 변형 과정 및 염색질 변형에 의해 매개되는 후성유전학적 조절도 연관되어 있다. 본 총설에서는 현재까지 보고된 물부족 스트레스 신호 전달 과정을, 이와 관련되어 보고된 다양한 신호 전달 단백질들의 기능과 연계시켜 알아보고자 한다. 이러한 물부족 스트레스 신호 전달 과정에 대한 명확한 이해는 향후 유용 내건성 작물 개발을 위한 이론적 기반 구축에 도움이 될 수 있을 것이라 생각된다.

설피리독신과 알파-만노시다제 간의 단백질 결합 특성에 관한 고찰 (Characterization of the Interaction of Sulfiredoxin (Srx1) with a Vacoular Protein $\alpha$-Mannosidase (Ams1) in Saccharomyces cerevisiae)

  • 바란독카랜;김일한
    • 자연과학논문집
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    • 제17권1호
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    • pp.13-29
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    • 2006
  • 산화-환원 활성 단백질중에 하나인 설피레독신과의 결합 단백질을 효모 Two-hybrid 기법을 이용하여 탐색한 결과, 알파-만노시다제가 설피레독신과 특이적으로 결합함을 밝혔다. 알파-만노시다제는 D-만노스 당을 비환원성 말단으로부터 유리시키는 가수분해 효소로서, 세포 원형질에 다량체 형태로 존재한다. 본 연구에서는 설피레독신과 알파-만노시다제간의 단백질결합을 설피레독신의 새로운 생리기능 관점에서 토의했다.

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