Method for Quantifying Oxidized Methionines and Application to HIV-1 Env

Shipman, J. J.; Go, Eden P.; Desaire, Heather

doi:10.1007/s13361-018-2010-2

Cited by 15 publications

(27 citation statements)

References 25 publications

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“…18 O 2 and the use of the ϩ2-Da mass shift arising from 18 O incorporation to differentiate artifactual oxidation from "real" oxidation (203). Although an improvement, this method still has problems with peptides containing multi-ple Met residues, but this may be resolved using a method employing theoretical isotope distributions (205). The use of significant levels of peroxide in this method may also induce other alterations.…”

Section: Detection and Quantification Of Productsmentioning

confidence: 99%

Detection, identification, and quantification of oxidative protein modifications

Hawkins

Davies

2019

Journal of Biological Chemistry

291

209

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Edited by Ruma Banerjee Exposure of biological molecules to oxidants is inevitable and therefore commonplace. Oxidative stress in cells arises from both external agents and endogenous processes that generate reactive species, either purposely (e.g. during pathogen killing or enzymatic reactions) or accidentally (e.g. exposure to radiation, pollutants, drugs, or chemicals). As proteins are highly abundant and react rapidly with many oxidants, they are highly susceptible to, and major targets of, oxidative damage. This can result in changes to protein structure, function, and turnover and to loss or (occasional) gain of activity. Accumulation of oxidatively-modified proteins, due to either increased generation or decreased removal, has been associated with both aging and multiple diseases. Different oxidants generate a broad, and sometimes characteristic, spectrum of post-translational modifications. The kinetics (rates) of damage formation also vary dramatically. There is a pressing need for reliable and robust methods that can detect, identify, and quantify the products formed on amino acids, peptides, and proteins, especially in complex systems. This review summarizes several advances in our understanding of this complex chemistry and highlights methods that are available to detect oxidative modifications-at the amino acid, peptide, or protein level-and their nature, quantity, and position within a peptide sequence. Although considerable progress has been made in the development and application of new techniques, it is clear that further development is required to fully assess the relative importance of protein oxidation and to determine whether an oxidation is a cause, or merely a consequence, of injurious processes.

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Section: Detection and Quantification Of Productsmentioning

confidence: 99%

Detection, identification, and quantification of oxidative protein modifications

Hawkins

Davies

2019

Journal of Biological Chemistry

291

209

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“…It should be noted that newer methodologies have since been developed that circumvent artifactual oxidation by 'blocking' unoxidized methionines using isotopically labelled oxidizing agents prior to mass spectrometric analysis ( Figure 2) [36,87,88]. This approach allows for accurate quantitation of in vivo methionine oxidation from tissue or cell extracts.…”

Section: Methionine Oxidation As a Clinical Feature Of Prion Diseasementioning

confidence: 99%

Methionine oxidation within the prion protein

Bettinger

Ghaemmaghami

2020

Prion

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Prion diseases are characterized by the self-templated misfolding of the cellular prion protein (PrP C) into infectious aggregates (PrP Sc). The detailed molecular basis of the misfolding and aggregation of PrP C remains incompletely understood. It is believed that the transient misfolding of PrP C into partially structured intermediates precedes the formation of insoluble protein aggregates and is a critical component of the prion misfolding pathway. A number of environmental factors have been shown to induce the destabilization of PrP C and promote its initial misfolding. Recently, oxidative stress and reactive oxygen species (ROS) have emerged as one possible mechanism by which the destabilization of PrP C can be induced under physiological conditions. Methionine residues are uniquely vulnerable to oxidation by ROS and the formation of methionine sulfoxides leads to the misfolding and subsequent aggregation of PrP C. Here, we provide a review of the evidence for the oxidation of methionine residues in PrP C and its potential role in the formation of pathogenic prion aggregates.

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“…N-terminal acetylation of proteins were described to affect protein stability [64]. In the case of N-terminal acetylation, a distinction between N α -acetylation and N ε -acetylation (lysine residue) has to be made.…”

Section: Identi Cation Of Different Post-translational Modi Cations Bmentioning

confidence: 99%

“…Interestingly, the only N-acetylation among Acb proteins was identi ed in the putative acarbose 4-alphaglucanotransferase AcbQ during the middle of the growth phase (T3; 72.3 h). Since N-terminal acetylation can affect the protein stability in both directions [64], it can be assumed that stability of AcbQ is posttranslational in uenced. Interestingly, AcbQ shows one of the most stable protein abundances among Acb proteins over the cultivation process (Fig.…”

Section: Identi Cation Of Different Post-translational Modi Cations Bmentioning

confidence: 99%

The expression of the acarbose biosynthesis gene cluster in Actinoplanes sp. SE50/110 is dependent on the growth phase

Droste

Ortseifen

Schaffert

et al. 2020

Preprint

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Background: Actinoplanes sp. SE50/110 is the natural producer of the diabetes mellitus drug acarbose, which is highly produced during the growth phase and ceases during the stationary phase. In previous works, the growth-dependency of acarbose formation was assumed to be caused by a decreasing transcription of the acarbose biosynthesis genes during transition and stationary growth phase.Results: In this study, transcriptomic data using RNA-seq and state-of-the-art proteomic data from seven time points of controlled bioreactor cultivations were used to analyze expression dynamics during growth of Actinoplanes sp. SE50/110. A hierarchical cluster analysis revealed co-regulated genes, which display similar transcription dynamics over the cultivation time. Aside from the expected metabolic switch from primary to secondary metabolism during transition phase, we observed a significantly decreasing transcript abundance of all acarbose biosynthetic genes, with the strongest decrease for the monocistronically transcribed genes acbA, acbB, acbD and acbE. Our data confirm a similar trend for acb gene transcription and acarbose formation rate.Surprisingly, the proteome dynamics does not follow the respective transcription for all acb genes. This suggests different protein stabilities or post-transcriptional regulation of the Acb proteins, which in turn could indicate bottlenecks in the acarbose biosynthesis. Furthermore, several genes are co-expressed with the acb gene cluster over the course of the cultivation, including eleven transcriptional regulators (e.g. ACSP50_0424), two sigma factors (ACSP50_0644, ACSP50_6006) and further genes, which have not previously been in focus of acarbose research in Actinoplanes sp. SE50/110.Conclusion: In conclusion, we have demonstrated, that a genome wide transcriptome and proteome analysis in a high temporal resolution is well suited to study the acarbose biosynthesis and the transcriptional and post-transcriptional regulation thereof.

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Method for Quantifying Oxidized Methionines and Application to HIV-1 Env

Cited by 15 publications

References 25 publications

Detection, identification, and quantification of oxidative protein modifications

Detection, identification, and quantification of oxidative protein modifications

Methionine oxidation within the prion protein

The expression of the acarbose biosynthesis gene cluster in Actinoplanes sp. SE50/110 is dependent on the growth phase

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