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Literature DB >> 17531489

A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates.

Abstract

O-GlcNAc transferase (OGT) catalyzes the addition of N-acetylglucosamine (O-GlcNAc) onto a diverse array of intracellular proteins. Although hundreds of proteins are known to be modified by O-GlcNAc, a strict amino acid consensus sequence for OGT has not been identified. In this study, we describe the development of a high-throughput assay for OGT and use it to profile the specificity of the enzyme among a panel of peptide substrates.

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Year: 2007 PMID： 17531489 PMCID： PMC3225185 DOI： 10.1016/j.bmcl.2007.05.008

Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823

26 in total

1. Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography.

Authors: S P Jackson; R Tjian
Journal: Proc Natl Acad Sci U S A Date: 1989-03 Impact factor: 11.205

2. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats.

Authors: L K Kreppel; G W Hart
Journal: J Biol Chem Date: 1999-11-05 Impact factor: 5.157

3. Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1.

Authors: G D Holt; R S Haltiwanger; C R Torres; G W Hart
Journal: J Biol Chem Date: 1987-11-05 Impact factor: 5.157

4. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

Authors: C R Torres; G W Hart
Journal: J Biol Chem Date: 1984-03-10 Impact factor: 5.157

5. Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling.

Authors: Matthew R Pratt; Howard C Hang; Kelly G Ten Hagen; Jason Rarick; Thomas A Gerken; Lawrence A Tabak; Carolyn R Bertozzi
Journal: Chem Biol Date: 2004-07

6. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.

Authors: R S Haltiwanger; M A Blomberg; G W Hart
Journal: J Biol Chem Date: 1992-05-05 Impact factor: 5.157

7. O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.

Authors: S P Jackson; R Tjian
Journal: Cell Date: 1988-10-07 Impact factor: 41.582

8. Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.

Authors: E P Roquemore; A Dell; H R Morris; M Panico; A J Reason; L A Savoy; G J Wistow; J S Zigler; B J Earles; G W Hart
Journal: J Biol Chem Date: 1992-01-05 Impact factor: 5.157

9. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability.

Authors: Niall O'Donnell; Natasha E Zachara; Gerald W Hart; Jamey D Marth
Journal: Mol Cell Biol Date: 2004-02 Impact factor: 4.272

10. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.

Authors: G D Holt; C M Snow; A Senior; R S Haltiwanger; L Gerace; G W Hart
Journal: J Cell Biol Date: 1987-05 Impact factor: 10.539

13 in total

1. Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.

Authors: Seok-Ho Yu; Michael Boyce; Amberlyn M Wands; Michelle R Bond; Carolyn R Bertozzi; Jennifer J Kohler
Journal: Proc Natl Acad Sci U S A Date: 2012-03-12 Impact factor: 11.205

2. Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.

Authors: David L Shen; Tracey M Gloster; Scott A Yuzwa; David J Vocadlo
Journal: J Biol Chem Date: 2012-02-06 Impact factor: 5.157

10. O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.

Authors: Zebulon G Levine; Chenguang Fan; Michael S Melicher; Marina Orman; Tania Benjamin; Suzanne Walker
Journal: J Am Chem Soc Date: 2018-03-05 Impact factor: 15.419

A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates.

1. Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography.

2. Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats.

3. Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1.

4. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

5. Deconvoluting the functions of polypeptide N-alpha-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling.

6. Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase.

7. O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.

8. Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.

9. Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability.

10. Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.

1. Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.

2. Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.

3. Broad spectrum O-linked protein glycosylation in the human pathogen Neisseria gonorrhoeae.

Review 4. Chemical and Biochemical Strategies To Explore the Substrate Recognition of O-GlcNAc-Cycling Enzymes.

5. Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes.

6. cat-ELCCA: catalyzing drug discovery through click chemistry.

7. Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.

8. Enzymatic glycosylation of peptide arrays on gold surfaces.

9. The active site of O-GlcNAc transferase imposes constraints on substrate sequence.

10. O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.