• Title/Summary/Keyword: 단백질 합성

Search Result 892, Processing Time 0.031 seconds

Thioredoxin-Mediated Regulation of Protein Synthesis by Redox in Saccharomyces cerevisiae (Saccharomyces cerevisiae에서 산화환원에 의한 In Vitro 단백질합성의 Thioredoxin에 중재된 조절)

  • Choi, Sang-Ki
    • Microbiology and Biotechnology Letters
    • /
    • v.35 no.1
    • /
    • pp.36-40
    • /
    • 2007
  • Redox signaling is one of way to regulate growth and death of cell in response to change of redox of proteins. To search whether translation is regulated by redox, we attempted in vitro translation assay under condition with or without DTT. Interestingly in vitro translation activity was increased up to 40% In the presence of dithiothreitol (DTT). Then we checked whether this positive effect by DTT was further accelerated by addition of thioredoxin (Trx). When a Trx purified from Saccharomyces cerevisiae was added to the in vitro translation extract, we observed a dose-dependent increase in translational activity. These results suggest the possibility of translation factors being redox-regulated via Trx in vivo.

Autoradiographic Studies on the Protein Synthesis in the egg chamber during Oogenesis of Drosophila melanogaster (노랑초파리의 난자형성에 따른 난실 내의 단백질 합성에 대한 자기방사적 연구)

  • 박성순;이양림
    • The Korean Journal of Zoology
    • /
    • v.38 no.2
    • /
    • pp.145-152
    • /
    • 1995
  • 노랑초파리의 난실에서의 단백질 합성을 난자형성과정의 단계별로 자기방사법을 이용하여 관찰하였다 단백질은 영양세포에서 난자형성 초기에 미약한 정도로 함성되는 것으로 나타나지만, 가장 활발하게 합성되는 세포는 여포세포이다. 난모세포와 영양세포에서는 단백질이 거의 합성되지 않고 있다. 여포세포에서 합성된 단백질은 Stage 10 이후의 단계에서만 난모세포로 이동하는 것으로 관찰되었다 난모세포에 괸만하게 분포된 은입자는 난자 형성을 위한 다양한 목적을 위해 여포세포로 부터 이입된 단백질로 짐작된다. 특히 난황립의 형성에 여포세포의 단백질이 최소한도 부분적으로 관여한다는 사실을 알 수 있었다.

  • PDF

Effects of Mutagens on the Synthetic Patterns of Proteins During the Early Developmental Stages in Mice (생쥐 초기배아의 단백질 합성양상에 미치는 돌연변이 유발원의 영향)

  • 이양림
    • The Korean Journal of Zoology
    • /
    • v.23 no.3
    • /
    • pp.149-160
    • /
    • 1980
  • The effects of mutagens, MMS and captan, on the patterns of proteins synthesized during the early developmental stages in mice were analyzed using two-dimensional electrophoresis. Three classes of proteins were observed in terms of synthetic pattern during the preimplantation stages. The first class is synthesized from the m-RNA, which was made and preserved throughout oogenesis and activated at the fertilization. The synthesis of these proteins did not seem to be influenced by MMS. The second class, which may be stagespecific proteins synthesized by newly transcribed m-RNA, was selectively inhibited by MMS. The third class, the synthesis of which is also suppressed by MMS, is the proteins synthesized by the m-RNA transcribed in augmented fashion. While MMS inhibits protein synthesis dependent on thenew transcription, this mutagen enhances a synthesis of a few proteins which were not observed in the untreated embryos. Captan did not affect protein synthesis at morula stage.

  • PDF

The a Domain of Protein Disulfide Isomerase is critical for synthesis of secretory proteins in Saccharomyces Cervisiae (Saccharomyces Cervisiae의 분비성 단백질의 합성 효율에 관여하는 이황이성질화 효소의 활성 도메인)

  • Kim, Sung-Hwan;Kim, Tae-Yoon;Kang, Ha-Ra
    • Proceedings of the KAIS Fall Conference
    • /
    • 2012.05a
    • /
    • pp.239-242
    • /
    • 2012
  • 효모 (Saccharomyces Cervisiae)는 단일 세포의 형태로 존재하는 진핵 세포로써 동물세포와 유사한 기작으로 분비성 단백질을 생성한다. 따라서 박테리아와 달리 효모를 이용하면 당단백질이나 이황결합을 포함하는 분비성 단백질을 경제적으로 대량 합성할 수 있다. 효모의 필수 단백질 중 하나인 단백질 이황이성질화 효소는 소포체에 위치하며 분비성 단백질에 구조적으로 안정한 이황결합을 제공하는 효소이다. 본 연구는 단백질 이황이성질화 효소 (protein disulfide isomerase)가 지니고 있는 두 개의 활성도메인 중 분비성 단백질들의 합성 효율에 직접적으로 관여하는 부위를 찾는 연구이다. 효모 유전체로부터 단백질 이황이성질화 효소의 유전자 (PDI1)을 제거하고 효소의 변이 유전자를 주입한 후 효모의 성장 속도를 측정하였다. 또한 효모의 대표적 분비성 단백질을 각 변이 효소를 지니는 효모에 과발현시켜 합성 및 이황결합 형성 효율을 측정하였다. 단백질 이황이성질화 효소내 두 개의 활성 부위 중 아미노 말단쪽에 위치한 a 도메인에 있는 활성 부위가 분비성 단백질의 활성에 중요한 역할을 한다는 것을 알 수 있었다. 이 결과는 이황결합이나 당을 포함하는 외래 단백질의 고효율 합성을 위한 새로운 효모종 개발에 중요한 정보를 제공할 것으로 기대 된다.

  • PDF

Beta-adrenergic regulation of the DNA Synthesis and Epidermal Growth Factor Secretion in cultured Submandibular Gland Cells (악하선 배양세포의 DNA합성 및 Epidermal Growth Factor분비에 관련된 Beta-adrenergic 조절에 관한 연구)

  • 이금영;소준노
    • The Korean Journal of Zoology
    • /
    • v.34 no.3
    • /
    • pp.410-419
    • /
    • 1991
  • 마우스 악하선 배양세포의 DNA와 단백질 합성 및 epidermal growth factor(EGF) 분비에 미치는 isoproterenol(IPR)의 효과를 조사하였다. 마우스 악하선으로부터 분리되어 배양된 상피형세포의 DNA및 단백질 합성은 IRP에 의해 농도 의존적으로 현저하게 감소하였다. 이와는 달리 IPR처리 1시간 후에 IPR-처리 마우스로부터 얻은 혈청은 악하선 배양세포의 단백질 합성에는 별 영향을 미치지 못하였으나, DNA합성은 현저하게 증가시켰다. IPR에 의한 악하선 세포의 DNA 합성능의 감소는 propranolol에 의해 차단되지 않았으나 ascorbate에 의해서는 회복되었다. 악하선 배양세포의 DNA 및 단백질 합성을 저해한 IPR의 처리에 의해 배양세포의 EGF분비는 현저히 증가되었다. 이상과 같은 결과는 악하선 세포의 DNA 및 단백질 합성에 작용한 IPR의 효과는 beta-adrenoceptor의 흥분에 의한 것이라기 보다는 IPR로부터 유래된 free radical에 의한 세포독성에 기인함을 시사한다. 따라서 IPR의 생체내 투여에 의한 악하선의 비대화를 보고 한 기존의 결과는 IPR이 악하선에 직접 작용하여 유발된 것이 아닌 다른 경로를 통한 간접적인 효과로 판단될 수 있을 것이다.

  • PDF

Changes of Protein Synthesis during Oogenesis of Drosophila melanogaster (노랑초파리의 난자형성과정에서의 단백질 합성의 변화)

  • 박성순;이양림
    • The Korean Journal of Zoology
    • /
    • v.30 no.1
    • /
    • pp.10-28
    • /
    • 1987
  • Changes of protein synthesis in the isolated egg chambers were studied during oogenesis of Drosophila melanogaster. Protein synthesis did not change much in quantity except that the activity was slightly enhanced at the stages 11 and 12, when new structures such as vitelline membranes and yolk granules were made, but considerably changed in quality during oogenesis. Protein synthesis was believed to occur mainly in the follicle cells, and a number of stage-specific proteins were found to differ at various stages. The observations suggest that proteins synthesized in the cells within chambers as well as those from the outside of the chambers might be directly required for the growth and maturation of oocytes in Drosophila.

  • PDF

Amplified synthesis and stability of Tn5 polypeptides in escherichia coli (대장균에서의 Tn5 단백질 증폭생합성 및 안정성)

  • 정재성;정재훈
    • Korean Journal of Microbiology
    • /
    • v.27 no.4
    • /
    • pp.323-333
    • /
    • 1989
  • Plasmid DNA molecules containing strong promoter upstream from IS50L or IS50R, the two insertion sequences that flank Tn5, were constructed to amplify the synthesis of Tn5-encoded polypeptides. When proteins made by cells that contain these plasmids were analyzed on polyacrylamide gels, enhanced synthesis of IS50R polypeptides could be detected. Synthesis of this polypeptide apparently is initiated within the large open reading frame of this element. In addition, the stability of IS50L-and IS50R-encoded polypeptides was analyzed. It was found that IS50L polypeptides are relatively unstable in vivo. This instability could account for the observed inability of this element to promote transposition.

  • PDF

Enhancement of Glucose-Fueled Cell-Free Protein Synthesis by the Addition of Lipids (지질의 첨가를 통한 포도당 기반 무세포 단백질 합성 시스템의 단백질 발현 효율 향상)

  • Lee, So Jeong;Kim, Ho-Cheol;Kim, Dong-Myung
    • Korean Chemical Engineering Research
    • /
    • v.57 no.1
    • /
    • pp.85-89
    • /
    • 2019
  • Cell-free protein synthesis utilizes the translational machinery in a cell extract. Unlike the conventional cell-based expression methods, not being affected by the conditions for cell growth, cell-free protein synthesis enables flexible manipulation of individual factors affecting the efficiency protein biosynthesis. However, the high cost and low stability of the energy sources to regenerate ATP have limited the use of cell-free synthesis for large-scale production of recombinant proteins. One of the approaches to address this problem is to use glucose as an alternative energy source to regenerate ATP through the glucose-metabolizing pathways in a cell extract. In this study, in an attempt to improve the efficiency of ATP regeneration by reinforcing oxidative phosphorylation process, we supplemented with cellular lipids to a glucose-fueled reaction mixture for cell-free protein synthesis. As a result of the lipid supplementation, the productivity of chloramphenicol acetyltransferase in a cell-free synthesis system using glucose increased more than 6 fold compared to when the lipid was not supplemented.

Changes in the RNA and Protein Synthesis at the Pre- and Post fertilization Stages of a Sea Urchin, Hemicentrotus pulcherrimus (말똥성게 (Hemicentrotus polcherrimus)의 수정전과 초기 발생동안 RNA 및 단백질합성의 변화)

  • Jang, Jeong-Won;Lee, Yang-Rim
    • The Korean Journal of Zoology
    • /
    • v.28 no.2
    • /
    • pp.71-84
    • /
    • 1985
  • Syntheses of RNA and protein were studied to examine changes in activating stored mRNAs during the early development of a sea urchin, Hemicentrotus pulcherimus. The rates of RNA and protein syntheses are very low in the unferilized eggs but the protein synthesis is activated upon the fertilization, while RNA synthesis remains still inactive at the same stage. These rates increase drastically at the blastula and gastrula stages, although the increases are not exactly in parallel. The protein synthesis was found to be also changing in quality during the early development from the studies by the two-dimensional gel electrophoresis.

  • PDF

Ovarian and Fat Body Yolk Protein Synthesis in Culex piplens pallens (홍모기(Culex pipiens pallens) 지방체와 난소에서의 난황단백질합성에 관한 연구)

  • 이승훈;박영민;성기창
    • The Korean Journal of Zoology
    • /
    • v.36 no.3
    • /
    • pp.416-424
    • /
    • 1993
  • Ovarian Yolk protein (YP2) synthesis has been investigated in mosquito, Culex pipiens pallens. Yolk protein amount which was syntheized in fat body, accumulated into ovary were analyzed by Rocket immunoelectrophoresis and in vitro organ culture. The result was that yolk protein synthesis began to occur at 6hrs after blood meal, reached at maximum level by 24hrs, and was completed within 48hrs. Yolk protein accmulation into the ovary began to start at 6hrs and coutinued for up to 60hrs after blood meal. Extract from 0, 24, 48, 72hrs ovaries after blood meal were analyzed by electrophoresis and Western blotting. The result was that 24hrs ovary contain one yolk protein(YP1), and 48, 72hrs ovaries contain two kinds of yolk proteins(YPl and YP2). When 48hr ovaries and fat bodies were incubated in $^3$H-leucine contained medium, protein synthesis was not occurred in fat body, but ovary synthesized much protein contained yolk protein (YP2). The result of crossed immunoelectrophoresis represented the same immunity between YPl and YP2. The present data suggest that ovary synthesize yolk protein(YP2) in mosquito, Culex pipiens pallens.

  • PDF