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Session V : 신진연구자, 좌장 : 추영국 교수 (원광대학교)
Functional and Molecular Characterization of PMT5 and PMT6 genes encoding Protein O-Mannosyltransferases in the Thermotolerant Methylotrophic Yeast Hansenula polymorpha
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- 발행기관
- 한국당과학회 바로가기
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- 간행물
- 한국당과학회 학술대회 바로가기
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- 통권
- 2013 한국당과학회 동계학술대회 (2013.02)바로가기
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- 페이지
- pp.35-35
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- 저자
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- 언어
- 영어(ENG)
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- URL
- https://www.earticle.net/Article/A212699
※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.
원문정보
초록
- 영어
- Protein O-mannosylation is evolutionarily conserved protein modification of fundamental importance, which is mediated by protein O-mannosyltransferases(Pmtproteins). The whole genome information of the thermotolerant methylotrophic yeast Hansenula polymorpha reveals the presence of five PMT homologues (HpPMT1, HpPMT2, HpPMT4, HpPMT5, and HpPMT6) encoding Pmt proteins, In this study, we carried out molecular characterization of HpPMT5 and HpPMT6, which show homologies to Saccharomyces cerevisiae PMT1 and PMT2 subfamily members, respectively. Although any detectable growth defects were not detected in the Hppmt5 and Hppmt6 single deletion mutants, they showed significantly increased sensitivity to the PMT1 inhibitor R3A-1c. As expected, the Hppmt1pmt5 and Hppmt1pmt6 double mutants became more susceptible to cell wall disturbing reagents, compared to the single Hppmt1 mutant. Furthermore, O-mannosylation of HpWsc1p and HpMid2p, the cell surface sensors of cell wall integrity-signaling, was significantly defected in the both Hppmt1pmt5 and Hppmt1pmt6 mutants. Interestingly, phosphorylaiton of Mpk1 protein, which results in the stimulation of the cell wall integrity pathway, was more markedly induced in the Hppmt1pmt5 than in Hppmt1 even under normal condition. The membrane fractionation experiment showed that all the HpPmt proteins are localized at the ER/Golgi membrane except HpPmt6p, which was mostly detected as soluble protein. By co-immunoprecipitation experiments, we confirmed the complex formation between HpPmt1p and HpPmt2p, but no interaction between HpPmt5p and HpPmt2p. Altogether, these results support that HpPmt5p and HpPmt6p have redundant functions to significantly compensate the loss of HpPmt1p in protein O-mannosylation that are essential for cell growth, cell wall integrity, and stress resistance of H. polymorpha.
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 2013 한국당과학회 동계학술대회
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