Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli.

Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Research Abstract Details 

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Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Abstract Text:

Ran Xu,Sarah R Hanson,Zhiwen Zhang,Yu-Ying Yang,Peter G Schultz,Chi-Huey Wong,

Glycosylation is a prevalent posttranslational process capable of augmenting and modulating protein function. Efficient synthesis of high-purity, homogeneous glycoproteins is essential for the study of unique protein glycoforms and for the manufacture of therapeutically relevant forms. A promising new strategy for controlled in vivo synthesis of glycoproteins was recently established using suppressor tRNA technology. Using an evolved tRNA aminoacyl synthetase-tRNA pair from Methanococcus jannaschii, the glycosyl amino acid, N-acetylglucosamine-beta-O-serine (GlcNAc-beta-Ser), was site-specifically introduced into proteins cotranslationally in Escherichia coli. Herein, we report the evolution of a new tRNA aminoacyl synthetase-tRNA pair that has expanded the repertoire of glycoproteins that can be expressed in E. coli to contain the other major O-linked glycan, N-acetylgalactosamine-alpha-O-threonine (GalNAc-a-Thr).

Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Publishing Authors By Initials

R Xu,SR Hanson,Z Zhang,YY Yang,PG Schultz,CH Wong,

For similar enzymes and coenzymes: enzymes: ligases: carbon-oxygen ligases: amino acyl-trna synthetases: tyrosine-trna ligase research abstracts see: enzymes and coenzymes: enzymes: ligases: carbon-oxygen ligases: amino acyl-trna synthetases: tyrosine-trna ligase research

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Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of the American Chemical Society

VOLUME: 126

Page Numbers: 15654-5

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 8

MONTH: Dec

YEAR: 2004

Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Tyrosine-tRNA Ligase

MESH TERMS: metabolism

Chemical & Substance for Abstract: Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli. Information

Substance Name: Tyrosine-tRNA Ligase

Registry Number: EC 6.1.1.1

Grant and Affiliation Information for Site-specific incorporation of the mucin-type N-acetylgalactosamine-alpha-O-threonine into protein in Escherichia coli.

AFFILIATION: Department of Chemistry, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 Torrey Pines Road, La Jolla, California 92037, USA.

Country: United States

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MEDLINETA: J Am Chem Soc

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