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  • 1
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    Production of complex human glycoproteins in yeast (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-30
    Description: We report the humanization of the glycosylation pathway in the yeast Pichia pastoris to secrete a human glycoprotein with uniform complex N-glycosylation. The process involved eliminating endogenous yeast glycosylation pathways, while properly localizing five active eukaryotic proteins, including mannosidases I and II, N-acetylglucosaminyl transferases I and II, and uridine 5'-diphosphate (UDP)-N-acetylglucosamine transporter. Targeted localization of the enzymes enabled the generation of a synthetic in vivo glycosylation pathway, which produced the complex human N-glycan N-acetylglucosamine2-mannose3-N-acetylglucosamine2 (GlcNAc2Man3GlcNAc2). The ability to generate human glycoproteins with homogeneous N-glycan structures in a fungal host is a step toward producing therapeutic glycoproteins and could become a tool for elucidating the structure-function relation of glycoproteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, Stephen R -- Bobrowicz, Piotr -- Bobrowicz, Beata -- Davidson, Robert C -- Li, Huijuan -- Mitchell, Teresa -- Nett, Juergen H -- Rausch, Sebastian -- Stadheim, Terrance A -- Wischnewski, Harry -- Wildt, Stefan -- Gerngross, Tillman U -- 1R43GM66690-1/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Aug 29;301(5637):1244-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Thayer School of Engineering and the Department of Biological Sciences, Dartmouth College, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12947202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalytic Domain ; Endoplasmic Reticulum/metabolism ; *Genetic Engineering ; Glycoproteins/*biosynthesis/chemistry/genetics ; Glycosylation ; Golgi Apparatus/metabolism ; Humans ; Mannosidases/*genetics/metabolism ; Membrane Transport Proteins/metabolism ; N-Acetylglucosaminyltransferases/metabolism ; Peptide Library ; Pichia/enzymology/*genetics/metabolism ; Polysaccharides/chemistry/*metabolism ; Protein Processing, Post-Translational ; Protein Transport ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/*biosynthesis ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Humanization of yeast to produce complex terminally sialylated glycoproteins (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-09
    Description: Yeast is a widely used recombinant protein expression system. We expanded its utility by engineering the yeast Pichia pastoris to secrete human glycoproteins with fully complex terminally sialylated N-glycans. After the knockout of four genes to eliminate yeast-specific glycosylation, we introduced 14 heterologous genes, allowing us to replicate the sequential steps of human glycosylation. The reported cell lines produce complex glycoproteins with greater than 90% terminal sialylation. Finally, to demonstrate the utility of these yeast strains, functional recombinant erythropoietin was produced.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, Stephen R -- Davidson, Robert C -- Sethuraman, Natarajan -- Nett, Juergen H -- Jiang, Youwei -- Rios, Sandra -- Bobrowicz, Piotr -- Stadheim, Terrance A -- Li, Huijuan -- Choi, Byung-Kwon -- Hopkins, Daniel -- Wischnewski, Harry -- Roser, Jessica -- Mitchell, Teresa -- Strawbridge, Rendall R -- Hoopes, Jack -- Wildt, Stefan -- Gerngross, Tillman U -- New York, N.Y. -- Science. 2006 Sep 8;313(5792):1441-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉GlycoFi Inc., 21 Lafayette Street, Suite 200, Lebanon, NH 03766, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16960007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cloning, Molecular ; Cytidine Monophosphate N-Acetylneuraminic Acid/metabolism ; Erythropoietin/chemistry/genetics/*metabolism ; Genetic Vectors ; Glycosylation ; Humans ; Pichia/*genetics/metabolism ; *Protein Engineering ; Rats ; Recombinant Proteins/biosynthesis/chemistry ; Sialic Acids/metabolism ; Sialoglycoproteins/*biosynthesis/chemistry/genetics ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    The telomeric transcriptome of Schizosaccharomyces pombe (2012)
    Oxford University Press
    Details
    Publication Date: 2012-04-15
    Description: Eukaryotic telomeres are transcribed into telomeric repeat-containing RNA (TERRA). Telomeric transcription has been documented in mammals, birds, zebra fish, plants and budding yeast. Here we show that the chromosome ends of Schizosaccharomyces pombe produce distinct RNA species. As with budding yeast and mammals, S. pombe contains G-rich TERRA molecules and subtelomeric RNA species transcribed in the opposite direction of TERRA (ARRET). Moreover, fission yeast chromosome ends produce two novel RNA species: C-rich telomeric repeat-containing transcripts (ARIA) and subtelomeric transcripts complementary to ARRET (αARRET). RNA polymerase II (RNAPII) associates with pombe chromosome ends in vivo and the telomeric factor Rap1 negatively regulates this association, as well as the cellular accumulation of RNA emanating from chromosome ends. We also show that the RNAPII subunit Rpb7 and the non-canonical poly(A) polymerases Cid12 and Cid14 are involved in the regulation of TERRA, ARIA, ARRET and αARRET transcripts. We confirm the evolutionary conservation of telomere transcription, and reveal intriguing similarities and differences in the composition and regulation of telomeric transcripts among model organisms.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 4
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    Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins (2006)
    American Association for the Advancement of Science
    Details
    Publication Date: 2006-09-08
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science
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