Earticle

초록

영어

We developed a method that uses lectin affinity chromatography to enrich glycosylated proteins where the modification terminates with N-acetyl-D-glucosamine (GlcNAc), and used this method in conjunction with ETD MS/MS to identify Arabidopsis proteins with this type of modification. We found forty-eight proteins with N-linked modification consisting of single GlcNAc attached by an N-linkage to the Asn of the Asn-X-Ser/Thr sequon that is commonly modified with larger N-linked oligosaccharides. An enzymatic and chemical labeling method that changes the mobility of GlcNAc modified protein during PAGE through addition of PEG was employed to investigate the origin N-GlcNAc modifications on the β-thioglucoside glucohydrolases (TGG1 and TGG2), which are both modified with multiple N-linked oligosaccharides. It has been hypothesized that N-GlcNAc modifications are produced when ENGase remove N-linked oligosaccharides. Arabidopsis has two ENGases (AtENGase85A and B). Through the analysis of AtENGase85A, AtENGase85B single and AtENGase85A/B double mutants, we discovered that the N-GlcNAc modification of TGG2 was greatly reduced by AtENGase85A, but TGG1 was not affected in any of the mutants. These results support that ENGase producing N-GlcNAc modifications by hydrolyze N-linked oligosaccharides but also suggest that some Arabidopsis N-GlcNAc modifications may be generated by another mechanism. Since N-GlcNAc modification was detected at only one site on each myrosinase, the production of the N-GlcNAc modification may be regulated.

목차

1. 학력
 2. 경력
 3. 주요 연구분야/공동연구 가능분야
 4. 수행중인 연구과제
 5. 대표 논문/특허
 6. 보유 기술, 장비 혹은 제공 가능한 물질(표준물질, 저해제, 효소, 항체, 유전자, 세포주등)
 Identification of Arabidopsis proteins with single N-GlcNAc modification
 Acknowledgement
 Reference

저자

• 김영천 [ Young-Cheon Kim | 제주대학교 아열대원예산업연구소, 연구교수 ]
• Neal Jahren [ Department of Plant Biology, Microbial and Plant Genomics Institute, 250 Biological Sciences Center, 1445 Gortner Ave., St. Paul MN 55108, USA ]
• Matthew D. Stone [ Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455 USA ]
• Namrata D. Udeshi [ Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA ]
• Todd W. Markowski [ Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455 USA, Center for Mass Spectrometry and Proteomics, University of Minnesota, St. Paul, MN 55108 USA ]
• BruceA. Witthuhn [ Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455 USA, Center for Mass Spectrometry and Proteomics, University of Minnesota, St. Paul, MN 55108 USA ]
• Jeffrey Shabanowitz [ Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA ]
• Donald F. Hunt [ Department of Chemistry, University of Virginia, Charlottesville, VA 22904, USA, Department of Pathology, University of Virginia, Charlottesville, VA 22904, USA ]
• Neil E. Olszewski [ Department of Plant Biology, Microbial and Plant Genomics Institute, 250 Biological Sciences Center, 1445 Gortner Ave., St. Paul MN 55108, USA ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614