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Identification of hydroxylation at aromatic amino acid residues in yeast kinase using mass spectrometry with affinity enrichment.
Zheng, Shuzhen; Bai, Xue; Tian, Shanshan; Wang, Guojuan; Zhai, Guijin; Guo, Zhenchang; Bi, Wenjing; Shen, Lijin; Zhang, Kai.
Affiliation
  • Zheng S; Department of Chemistry, Nankai University, Tianjin, 300071, China.
  • Bai X; Department of Chemistry, Nankai University, Tianjin, 300071, China.
  • Tian S; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
  • Wang G; Department of Chemistry, Nankai University, Tianjin, 300071, China.
  • Zhai G; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
  • Guo Z; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
  • Bi W; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
  • Shen L; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
  • Zhang K; 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical Epigenetics, Department of Biochemistry and Molecular Biology, Tianjin Medical University, Tianjin, 300070, China.
Rapid Commun Mass Spectrom ; 30 Suppl 1: 185-9, 2016 08.
Article in En | MEDLINE | ID: mdl-27539436
ABSTRACT
RATIONALE Protein kinases represent the key elements in phosphorylation-based signal transmission. Recent studies suggest that hydroxylation may mediate activities of protein kinases. This paper aims to examine the hydroxylation in protein kinases for improving our understanding of the protein modification.

METHODS:

We combined affinity-based protein purification with MS analysis for identification of novel hydroxylation at aromatic amino acid residues in yeast kinases.

RESULTS:

We identified 17 hydroxylation at aromatic amino acid residues (10 at Phe, 1 at Tyr and 6 at Trp) using MS analysis. We further characterized the localization and studied the potential significance of these modifications.

CONCLUSIONS:

This is a new report on the identification of hydroxylation at aromatic amino acid residues in yeast kinases. This study expands the catalog of hydroxylation in kinases and suggests the potential function of hydroxylation. Copyright © 2016 John Wiley & Sons, Ltd.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinases / Amino Acids, Aromatic / Saccharomyces cerevisiae Proteins / Tandem Mass Spectrometry Type of study: Diagnostic_studies Language: En Journal: Rapid Commun Mass Spectrom Year: 2016 Document type: Article Affiliation country: China
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Kinases / Amino Acids, Aromatic / Saccharomyces cerevisiae Proteins / Tandem Mass Spectrometry Type of study: Diagnostic_studies Language: En Journal: Rapid Commun Mass Spectrom Year: 2016 Document type: Article Affiliation country: China