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PP-3, Session 2: Glycobiology II, Chairperson: Chun-Hung Lin, Sopit Wongkham

Marine Invertebrate Sialyltransferase: Identification and Functional Characterization of a β-Galactoside α2,3-Sialyltransferase, Csav-ST3Gal I/II, from the Sea Squirt Ciona savignyi

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    ACGG 2012 Conference (2012.10)바로가기
  • 페이지
    pp.38-38
  • 저자
    Seonghun Kim, Doo-Byoung Oh, Hyun Ah Kang, Youn-Ho Lee, Ohsuk Kwon
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A192793

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원문정보

초록

영어
Sialyltransferase is a glycosyltransferase transferring sialic acid from CMP-Neu5Ac to the non-reducing terminal position of glycoconjugates. Twenty different sialyltransferases containing so-called sialylmotifs are highly conserved from invertebrates to vertebrates. These well conserved sialylmotifs suggested that all sialyltransferases had been evolved from a common ancestor. Many sialyltransferases have been known in vertebrate linage, however, only a few have been characterized in non-vertebrates. In this study, we cloned a gene encoding sialyltransferase (ST) from marine invertebrate organism, Ciona savignyi (Csav), and analyzed its phylogenetic relationship with other animal sialyltransferases. Csav-ST was clustered with ST3Gal subfamily. Csav-ST has two putative transcript isoforms identified in of the sea squirt C. savignyi genome database. To indentify a sialyltransferase activity, Csav-ST3Gal was functionally characterized by using recombinant enzyme expressed in Saccharomyces cerevisiae. Csav-ST3Gal is localized to Golgi membrane when expressed in yeast. Enzymatic assays indicate that Csav-ST3Gal is capable of transferring sialic acids to the glycans attached to asialofetuin. Substrate specificities and kinetic properties indicated that Csav-ST3Gal could prefer O-glycans rather than N-glycan of asialoglycoproteins as substrates. Further, it has been displayed that Csav-ST3Gal catalyzes the formation of α(2,3)-linkage by a lectin blot analysis with Maackia amurensis lectin and by the linkage-specific sialidase treatments. In addition, Csav-ST3Gal has three putative N-glycosylation sites in its stem region, Interestingly, only one site for N-glycosylation was occupied with N-glycan when expressed in yeast. By N-glycan trimming with glycosidases treatments, we determined that this glycan of Csav-ST could not be required for in vitro enzyme activity, because of no difference in non-glycosylated and glycosylated sialyltransferase activities. These results indicate that Csav-ST3Gal could be an common ancestral glycosyltransferase belonged to ST3Gal I/II subfamily, transferring sialic acid to Gal-β1,3-GalNAc moiety.

저자

  • Seonghun Kim [ Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology ]
  • Doo-Byoung Oh [ Systems and Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, KOREA ]
  • Hyun Ah Kang [ Department of Life Science, Chung-Ang University ]
  • Youn-Ho Lee [ Korea Ocean Research and Development Institute ]
  • Ohsuk Kwon [ Systems and Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, KOREA ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 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

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

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