Identification of N-homocysteinylation sites in plasma proteins

Sikora, Marta; Marczak, Łukasz; Kubalska, Jolanta; Graban, Ałła; Jakubowski, Hieronim

doi:10.1007/s00726-013-1617-7

Cited by 36 publications

(38 citation statements)

References 30 publications

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“…This left five peptides that could contain both the ‐C(O)CH 2 OH fragment from the linker of 10 and a missed cleavage site (Table S4, Table S5). Each missed cleavage site is a Lys or an Arg residue that is also a known glycation (K190, K351, K536, K541, R222, R472) site . Trypsin does not cleave the protein after a modified Lys or Arg residue.…”

Section: Resultsmentioning

confidence: 99%

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Tormyshev

Chubarov

Krumkacheva

et al. 2020

Chemistry A European J

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Trityl radicals (TAMs) have recently appeared as an alternative source of spin labels for measuring long distances in biological systems. Finland trityl radical (FTAM) served as the basis for this new generation of spin labels, but FTAM is rather lipophilic and susceptible to self‐aggregation, noncovalent binding with lipophilic sites of proteins, and noncovalent docking at the termini of duplex DNA. In this paper the very hydrophilic OX063 TAM with very low toxicity and little tendency for aggregation is used as the basis for a spin label. Human serum albumin (HSA) labeled with OX063 has an intense narrow line typical of TAM radicals in solution, whereas HSA labeled with FTAM shows broad lines and extensive aggregation. In pulse EPR measurements, the measured phase memory time TM for HSA labeled with OX063 is 6.3 μs at 50 K, the longest yet obtained with a TAM‐based spin label. The lowered lipophilicity also decreases side products in the labeling reaction.

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Section: Resultsmentioning

confidence: 99%

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Tormyshev

Chubarov

Krumkacheva

et al. 2020

Chemistry A European J

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“…N-homocysteinylation of plasma proteins has been largely documented [51]. However, little is known on the physiological role of S-homocysteinylation on intracellular proteins [47,52].…”

Section: Resultsmentioning

confidence: 99%

Peroxiredoxin post-translational modifications by redox messengers

Riquier¹,

Bretón²,

Abbas³

et al. 2014

Redox Biology

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Peroxiredoxins (Prxs) are a family of thiol peroxidases that participate in hydroperoxide detoxification and regulates H2O2 signaling. In mammals, the four typical 2-Cys Prxs (Prxs 1, 2, 3 and 4) are known to regulate H2O2-mediated intracellular signaling. The 2 catalytic cysteines of 2-Cys Prxs, the so-called peroxidatic and resolving cysteines, are regulatory switches that are prone to react with redox signaling molecules. We investigated the respective modifications induced by H2O2, NO and H2S in the murine macrophage cell line RAW264.7 by mass spectrometry and immunoblotting after separating 2-Cys Prxs by one-dimensional or two-dimensional PAGE. We found that H2S, unlike NO, does not prevent H2O2-mediated sulfinylation of 2-Cys Prxs and that Prx2 is more sensitive to NO-mediated protection against sulfinylation by peroxides. We also observed that cells exposed to exogenous NO, released by Cys-SNO or DETA-NO, or producing NO upon stimulation by IFN-γ and LPS, present an acidic form of Prx1 whose modification is consistent with S-homocysteinylation of its peroxidatic cysteine.

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“…Peptide sequence a,b N-Hcy site H3(10-26) K.STGGK*APRK(me3)QLATK(Ac)AAR.K K14 H3 (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26) K.APRK*QLATKAAR.K K18 H3 (18)(19)(20)(21)(22)(23)(24)(25)(26) R.K*QLATK(pro)AAR.K K18 H3 (18)(19)(20)(21)(22)(23)(24)(25)(26)(27) R.K(pro)QLATK*AARK(me1).S K23 …”

Section: Rangementioning

confidence: 99%

“…A mass tolerance of 10 ppm and 0.2 Da was used for the MS/MS tolerance 16. A mass tolerance of 10 ppm and 0.2 Da was used for the MS/MS tolerance 16.…”

mentioning

confidence: 99%

Crosstalk of homocysteinylation, methylation and acetylation on histone H3

Chen

Gao

et al. 2015

Analyst

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Homocysteine (hcy) is an intermediate metabolite in the metabolic pathway of cysteine and methionine. As a non-coded amino acid, hcy is not normally incorporated into protein. However, homocysteine can be recognized and activated by methionyl-tRNA synthetase (MetRs) to produce Hcy-thiolactone (HTL), which can react with the ε-amino group of a protein lysine residue. The N-hcy-linked protein carrying a free thiol group can influence protein structure and function, thus leading to severe diseases. Histone has multiple specific dynamic post-translational modifications (PTMs), especially on the N-terminal tail of histones enriched with lysine and arginine residues. In this study, we confirmed that histone H3 can be modified by HTL on lysine residue. Relative and absolute quantification methods based on mass spectrometry demonstrated the crosstalk between methylation and acetylation of H3 in response to excess HTL. Overall, our data provide novel insights into histone modifications and the regulatory mechanisms of diseases related to homocysteinylation.

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Identification of N-homocysteinylation sites in plasma proteins

Cited by 36 publications

References 30 publications

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Peroxiredoxin post-translational modifications by redox messengers

Crosstalk of homocysteinylation, methylation and acetylation on histone H3

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