Mass Spectrometry Following Mild Enzymatic Digestion Reveals Phosphorylation of Recombinant Proteins in Escherichia coli Through Mechanisms Involving Direct Nucleotide Binding-Reference-Cited by-同舟云学术

Mass Spectrometry Following Mild Enzymatic Digestion Reveals Phosphorylation of Recombinant Proteins in Escherichia coli Through Mechanisms Involving Direct Nucleotide Binding

Published:2010-05-11 Issue:6 Volume:9 Page:3311-3318
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

She Yi-Min¹,Xu Xiaohui¹,Yakunin Alexander F.¹,Dhe-Paganon Sirano¹,Donald Lynda J.¹,Standing Kenneth G.¹,Lee Daniel C.¹,Jia Zongchao¹,Cyr Terry D.¹

Affiliation:

1. Centre for Biologics Research, Biologics and Genetic Therapies Directorate, Health Canada, Ottawa, Ontario K1A 0K9, Canada, Banting and Best Department of Medical Research, and Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L6, Canada, Department of Chemistry and Department of Physics and Astronomy, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada, and Department of Biochemistry, Queen’s University, Kingston, Ontario K7L 3N6, Canada

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr9011987

Reference19 articles.

1. Mass Spectrometry as a Tool for Protein Crystallography

2. Spontaneous α-N-6-Phosphogluconoylation of a “His Tag” inEscherichia coli:The Cause of Extra Mass of 258 or 178 Da in Fusion Proteins

3. Post-translational modification of the N-terminal His tag interferes with the crystallization of the wild-type and mutant SH3 domains from chicken src tyrosine kinase

4. Tandem mass spectrometry of multiply phosphorylated forms of a ?histidine-tag? derived from a recombinant protein kinase expressed in bacteria

5. Phosphorylation of serine residues in histidine-tag sequences attached to recombinant protein kinases: A cause of heterogeneity in mass and complications in function

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