Periodate-Triggered Cross-Linking of DOPA-Containing Peptide−Protein Complexes

Burdine, Lyle; Gillette, Thomas G.; Lin, H.‐J.; Kodadek, Thomas

doi:10.1021/ja045982c

Cited by 73 publications

(79 citation statements)

References 17 publications

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“…[11][12][13] The hydroxyl groups in the molecule might enhance the H/D exchange due to their electron-donating properties. H/D exchange of about 90% takes place at three exchangeable sites on the benzene ring at 0°C or room temperature within 20 min in TfOD as see in the 1 H-NMR measurement (Fig.…”

Section: Resultsmentioning

confidence: 99%

Hydrogen/deuterium exchange of cross-linkable α-amino acid derivatives in deuterated triflic acid

Wang

Murai

Yoshida

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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In this paper we report here a hydrogen/deuterium exchange (H/D exchange) of cross-linkable α-amino acid derivatives with deuterated trifluoromethanesulfonic acid (TfOD). H/D exchange with TfOD was easily applied to o-catechol containing phenylalanine (DOPA) within an hour. A partial H/D exchange was observed for trifluoromethyldiazirinyl (TFMD) phenylalanine derivatives. N-Acetylprotected natural aromatic α-amino acids (Tyr and Trp) were more effective in H/D exchange than unprotected ones. The N-acetylated TFMD phenylalanine derivative afforded slightly higher H/D exchange than unprotected derivatives. An effective post-deuteration method for cross-linkable α-amino acid derivatives will be useful for the analysis of biological functions of bioactive peptides and proteins by mass spectrometry.

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Section: Resultsmentioning

confidence: 99%

Hydrogen/deuterium exchange of cross-linkable α-amino acid derivatives in deuterated triflic acid

Wang

Murai

Yoshida

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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“…Cross-linking/Label Transfer Reactions-Cross-linking followed by label transfer to detect DOPA-Gal4 AD/proteasome interactions have been described (20,21). The proteins indicated in the figure were added to the reaction mix at the same time as peptide addition.…”

Section: Methodsmentioning

confidence: 99%

“…Experiments that included GST-Gal4-VP16 to dissociate 26 S proteasome were done as above, but 100 nM GST-Gal4-VP16 was added to the proteasome for 15 min at room temperature before adding mono-Ub and completing the reaction. The experiment conducted to identify the targets of Ub in the proteasome was scaled up 5-fold relative to that described above (20,21).…”

Section: Methodsmentioning

confidence: 99%

“…2A). Extensive control experiments have revealed that cross-linking occurs only when the DOPA-containing molecule and the receptor are closely associated (21,25). When the cross-linked products are boiled in a dithiol-containing buffer prior to electrophoresis, the FlAsH-CCPGCC association is disrupted, resulting in transfer of the biotinylated FlAsH-DOPA reagent to the receptor protein ( Fig.…”

Section: Ub Antagonizes Proteasome-mediated Destabilization Inmentioning

confidence: 99%

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Physical and Functional Interactions of Monoubiquitylated Transactivators with the Proteasome

Archer

Burdine

Liu

et al. 2008

Journal of Biological Chemistry

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Destabilization of activator-DNA complexes by the proteasomal ATPases can inhibit transcription by limiting activator interaction with DNA. Modification of the activator by monoubiquitylation protects the activator from this destabilization activity. In this study, we probe the mechanism of this protective effect of monoubiquitylation. Using novel label transfer and chemical cross-linking techniques, we show that ubiquitin contacts the ATPase complex directly, apparently via Rpn1 and Rpt1. This interaction results in the dissociation of the activation domain-ATPase complex via an allosteric process. A model is proposed in which activator monoubiquitylation serves to limit the lifetime of the activator-ATPase complex interaction and thus the ability of the ATPases to unfold the activator and dissociate the protein-DNA complex.

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“…For periodate-mediated crosslinking, a final concentration of 1.0 mM NaIO 4 was added to the mixture and incubated for 2 min. A final concentration of 100 mM DTT was used to quench the reaction (26). The cross-linked membranes were washed three times with CAPS buffer (Sigma) (10 mM, pH 10) by centrifugation to remove non-bound Bio-DOPA.…”

Section: Dopa Chemical Cross-linkingmentioning

confidence: 99%

Identification of Residue-to-residue Contact between a Peptide Ligand and Its G Protein-coupled Receptor Using Periodate-mediated Dihydroxyphenylalanine Cross-linking and Mass Spectrometry

Umanah

Huang

Ding

et al. 2010

Journal of Biological Chemistry

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G protein-coupled receptors (GPCRs)4 comprise the largest family of cell surface proteins present in the human genome responsible for communication between the internal and external environments in response to signal molecules, including hormones, pheromones, and neurotransmitters. GPCRs are characterized by the presence of seven membrane-spanning helical segments separated by alternating intracellular and extracellular loop regions (1-3). Despite their diverse ligands, all GPCRs perform similar functions, coupling the binding of ligands to the activation of specific heterotrimeric guanine nucleotide-binding proteins (G proteins), leading to the modulation of downstream effector proteins and molecules. Due to their involvement in a multitude of physiological functions, GPCRs are targeted by ϳ50% of the human drugs currently marketed (1,4,5). Detailed information about GPCR-ligand interactions is critical for our understanding of GPCR-ligand binding and function.Despite the differences in the binding mechanisms of various ligand groups in the GPCR family, there are some similarities that span this superfamily of proteins (1, 3, 6 -8). Ligand binding triggers conformational changes at the extracellular and transmembrane regions of the receptor, which are then propagated to the cytoplasmic surfaces, leading to G protein coupling and activation. Thus, ligand binding leads to the alteration of existing interhelical interactions, thereby promoting a set of new interactions that leads to a energetically favorable activated conformational state of the receptor (8, 9). Large ligands, such as proteins, bind to the extracellular loops of GPCRs, whereas small molecules like adrenergic agents bind within the transmembrane region of the receptor. Within the peptide-binding GPCRs, a combination of ligand binding to the extracellular loops followed by ligand penetra-

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Periodate-Triggered Cross-Linking of DOPA-Containing Peptide−Protein Complexes

Cited by 73 publications

References 17 publications

Hydrogen/deuterium exchange of cross-linkable α-amino acid derivatives in deuterated triflic acid

Hydrogen/deuterium exchange of cross-linkable α-amino acid derivatives in deuterated triflic acid

Physical and Functional Interactions of Monoubiquitylated Transactivators with the Proteasome

Identification of Residue-to-residue Contact between a Peptide Ligand and Its G Protein-coupled Receptor Using Periodate-mediated Dihydroxyphenylalanine Cross-linking and Mass Spectrometry

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