| Structure of a hydroxyproline (Hyp)-arabinogalactan polysaccharide from repetitive Ala-Hyp expressed in transgenic Nicotiana tabacum. | |
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MedLine Citation:
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PMID: 14724279 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A synthetic gene encoding the fusion protein (Ala-Hyp)(51)-enhanced green fluorescent protein expressed in Nicotiana tabacum cells produced a fusion glycoprotein with all proline residues hydroxylated and substituted with an arabinogalactan polysaccharide. Alkaline hydrolysis of the fusion glycoprotein yielded a population of hydroxyproline (Hyp)-arabinogalactan polysaccharides ranging in size from 13 to 26 saccharide residues/Hyp, with a median size of 15-17 residues. We isolated a 15-residue Hyp-arabinogalactan for structure determination by sugar analyses and one- and two-dimensional nuclear magnetic resonance techniques that provided the assignment of proton and carbon signals of a small polysaccharide O-linked to the hydroxyl group of Hyp. The polysaccharide consisted of a 1,3-linked beta-D-Galp backbone with a single 1,6-linked beta-D-Galp "kink." The backbone had two side chains of Galp substituted at position 3 with an arabinose di- or trisaccharide and at position 6 with glucuronic acid or rhamnosyl glucuronic acid. Energy-minimized space-filling molecular models showed hydrogen bonding within polysaccharides attached to repetitive Ala-Hyp and also between polysaccharides and the peptide backbone. Polysaccharides distorted the peptide Ramachandran angles consistent with the circular dichroic spectra of isolated (Ala-Hyp)(51) and its reversion to a polyproline II-like helix after deglycosylation. This first complete structure of a Hyp-arabinogalactan polysaccharide shows that computer-based molecular modeling of Hyp-rich glycoproteins is now feasible and supports the suggestion that small repetitive subunits comprise larger arabinogalactan polysaccharides. |
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Authors:
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Li Tan; Feng Qiu; Derek T A Lamport; Marcia J Kieliszewski |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. Date: 2004-01-14 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 279 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2004 Mar |
Date Detail:
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Created Date: 2004-03-22 Completed Date: 2004-05-07 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 13156-65 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry, Ohio University, Athens, OH 45701, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Carbon
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chemistry Circular Dichroism Galactans / chemistry* Glucuronic Acid / chemistry Glycosylation Green Fluorescent Proteins Hydrolysis Hydroxyproline / chemistry* Luminescent Proteins / metabolism Magnetic Resonance Spectroscopy Models, Chemical Models, Molecular Polysaccharides / chemistry* Proline / chemistry Recombinant Fusion Proteins / chemistry Tobacco / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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2P41 RR 05351-06/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Galactans; 0/Luminescent Proteins; 0/Polysaccharides; 0/Recombinant Fusion Proteins; 147-85-3/Proline; 147336-22-9/Green Fluorescent Proteins; 51-35-4/Hydroxyproline; 576-37-4/Glucuronic Acid; 7440-44-0/Carbon; 9036-66-2/arabinogalactan |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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