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A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes

Xavier Hanoulle, Jozef Van Damme (UGent) , An Staes (UGent) , Lennart Martens (UGent) , Marc Goethals (UGent) , Joël Vandekerckhove (UGent) and Kris Gevaert (UGent)
(2006) JOURNAL OF PROTEOME RESEARCH. 5(12). p.3438-3445
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Abstract
Adenine nucleotides are small, abundant molecules that bind numerous proteins involved in pivotal cellular processes. These nucleotides are co-factors or substrates for enzymes, regulators of protein function, or structural binding motifs. The identification of nucleotide-binding sites on a proteome-wide scale is tempting in view of the high number of nucleotide-binding proteins, their large in vivo concentration differences, and the various functions they exert. Here, we report on a functional, chemical, gel-free proteomics technology that allows the identification of protein adenine nucleotide-binding site(s) in cell lysates. Our technology uses a synthetic ATP analogue, 5'-rho-fluorosulfonylbenzoylad-enosine (FSBA), as an affinity/activity-based probe for nucleotide-binding sites. When applied on a cellular level, 185 different FSBA-labeled sites in a human Jurkat cell lysate were identified. Functional and structural aspects of the use of FSBA on a proteome-wide scale are discussed.
Keywords
ADENOSINE, 5 '-p-fluorosulfonylbenzoyladenosine (FSBA), MASS-SPECTROMETRY, functional proteomics, affinity/activity-based probe, gel-free proteomics, diagonal chromatography, DEPENDENT PROTEIN-KINASE, ACTIVITY-BASED PROBES, TYROSINE PHOSPHORYLATION, IDENTIFICATION, ATP, CHROMATOGRAPHY, INACTIVATION, INHIBITOR

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Chicago
Hanoulle, Xavier, Jozef Van Damme, An Staes, Lennart Martens, Marc Goethals, Joël Vandekerckhove, and Kris Gevaert. 2006. “A New Functional, Chemical Proteomics Technology to Identify Purine Nucleotide Binding Sites in Complex Proteomes.” Journal of Proteome Research 5 (12): 3438–3445.
APA
Hanoulle, X., Van Damme, J., Staes, A., Martens, L., Goethals, M., Vandekerckhove, J., & Gevaert, K. (2006). A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes. JOURNAL OF PROTEOME RESEARCH, 5(12), 3438–3445.
Vancouver
1.
Hanoulle X, Van Damme J, Staes A, Martens L, Goethals M, Vandekerckhove J, et al. A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes. JOURNAL OF PROTEOME RESEARCH. 2006;5(12):3438–45.
MLA
Hanoulle, Xavier, Jozef Van Damme, An Staes, et al. “A New Functional, Chemical Proteomics Technology to Identify Purine Nucleotide Binding Sites in Complex Proteomes.” JOURNAL OF PROTEOME RESEARCH 5.12 (2006): 3438–3445. Print.
@article{356960,
  abstract     = {Adenine nucleotides are small, abundant molecules that bind numerous proteins involved in pivotal cellular processes. These nucleotides are co-factors or substrates for enzymes, regulators of protein function, or structural binding motifs. The identification of nucleotide-binding sites on a proteome-wide scale is tempting in view of the high number of nucleotide-binding proteins, their large in vivo concentration differences, and the various functions they exert. Here, we report on a functional, chemical, gel-free proteomics technology that allows the identification of protein adenine nucleotide-binding site(s) in cell lysates. Our technology uses a synthetic ATP analogue, 5'-rho-fluorosulfonylbenzoylad-enosine (FSBA), as an affinity/activity-based probe for nucleotide-binding sites. When applied on a cellular level, 185 different FSBA-labeled sites in a human Jurkat cell lysate were identified. Functional and structural aspects of the use of FSBA on a proteome-wide scale are discussed.},
  author       = {Hanoulle, Xavier and Van Damme, Jozef and Staes, An and Martens, Lennart and Goethals, Marc and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {ADENOSINE,5 '-p-fluorosulfonylbenzoyladenosine (FSBA),MASS-SPECTROMETRY,functional proteomics,affinity/activity-based probe,gel-free proteomics,diagonal chromatography,DEPENDENT PROTEIN-KINASE,ACTIVITY-BASED PROBES,TYROSINE PHOSPHORYLATION,IDENTIFICATION,ATP,CHROMATOGRAPHY,INACTIVATION,INHIBITOR},
  language     = {eng},
  number       = {12},
  pages        = {3438--3445},
  title        = {A new functional, chemical proteomics technology to identify purine nucleotide binding sites in complex proteomes},
  url          = {http://dx.doi.org/10.1021/pr060313e},
  volume       = {5},
  year         = {2006},
}

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