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ATP synthase β subunit is the first identified an O-GlcNAcylated protein from mitochondria of Drosophila
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- 발행기관
- 한국당과학회 바로가기
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- 간행물
- 한국당과학회 학술대회 바로가기
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- 통권
- 2008 Eastern Asian Glycoscience Symposium (2008.11)바로가기
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- 페이지
- pp.62-63
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- 저자
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- 언어
- 영어(ENG)
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- URL
- https://www.earticle.net/Article/A192331
※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.
원문정보
초록
- 영어
- β-O-linked N-acetylglucosamine (O-GlcNAc) addition is dynamic post-translational modification in nucleocytoplasmic proteins such as transcription factors, cytoskeletal proteins, and various enzymes. These proteins are modified with O-GlcNAc on their Ser/Thr residues and this event changes their intracellular functions, including transcription, proliferation, apoptosis, cell signaling. This modification takes place at the same sites as does phosphrylation or at adjacent residues. Like phosphorylation, protein O-GlcNAcylation dramatically alters the post translational fate and function of target proteins. Knock-out of the O-GlcNAc transferase (the nucleocytoplasmic enzymes for the addition of O-GlcNAc) result in stem cell and embryonic lethality so O-GlcNAc metabolism in Drosophila melanogaster will likely provide important clues to the cellular functions of O-GlcNAc modification. In order to detect O-linked GlcNAc modifications in Drosophila SL2 cell, immuno- blotting were performed with CTD 110.6 antibody. O-GlcNAcylated proteins in Drosophila SL2 cell were analyzed using two-dimensional gel electrophoresis and MALDI-TOF-MS. As a result, ATP synthase β subunit was identified as a novel O- GlcNAcylated protein in Drosophila SL2 cell. To confirm O-GlcNAcylation, immuno- blotting was performed with ATP synthase β antibody after SWGA lectin precipitation. Also, immuno-blotting was performed with ATP synthase β antibody and CTD 110.6 antibody after immuno-precipitation with CTD 110.6 antibody and ATP synthase β antibody, respectively. ATP synthase β subunit is encoded in the nucleus, synthesized in the cytosol and imported in to the mitochondria. ATP synthase β was identified in the mitochondria when we performed immunoblotting with CTD 110.6 antibody after organelle fractionation. Thus we will focus on revealing how ATP synthase β is modified with O-GlcNAc and what the functional roles of O-GlcNAcylation on ATP synthase β are.
저자
간행물 정보
발행기관
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- 발행기관명
- 한국당과학회 [Korean Society for Glycoscience]
- 설립연도
- 2006
- 분야
- 의약학>약학
- 소개
- 본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.
간행물
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- 간행물명
- 한국당과학회 학술대회
- 간기
- 연간
- 수록기간
- 2006~2022
- 십진분류
- KDC 517 DDC 614
이 권호 내 다른 논문 / 한국당과학회 학술대회 2008 Eastern Asian Glycoscience Symposium
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