scholarly journals Cysteine oxidation to the sulfinic acid induces oxoform-specific lanthanide binding and fluorescence in a designed peptide

2020 ◽  
Vol 152 ◽  
pp. 166-174
Author(s):  
Andrew R. Urmey ◽  
Neal J. Zondlo
2016 ◽  
Author(s):  
Mark D. White ◽  
Maria Klecker ◽  
Richard J. Hopkinson ◽  
Daan Weits ◽  
Carolin Mueller ◽  
...  

AbstractCrop yield loss due to flooding is a threat to food security. Submergence-induced hypoxia in plants results in stabilisation of group VII ETHYLENE RESPONSE FACTORS (ERF-VIIs), which aid survival under these adverse conditions. ERF-VII stability is controlled by the N-end rule pathway, which proposes that ERF-VII N-terminal cysteine oxidation in normoxia enables arginylation followed by proteasomal degradation. The PLANT CYSTEINE OXIDASEs (PCOs) have been identified as catalysts of this oxidation. ERF-VII stabilisation in hypoxia presumably arises from reduced PCO activity. We directly demonstrate that PCO dioxygenase activity produces Cys-sulfinic acid at the N-terminus of an ERF-VII peptide, which then undergoes efficient arginylation by an arginyl transferase (ATE1). This is the first molecular evidence showing N-terminal Cys-sulfinic acid formation and arginylation by N-end rule pathway components, and the first ATE1 substrate in plants. The PCOs and ATE1 may be viable intervention targets to stabilise N-end rule substrates, including ERF-VIIs to enhance submergence tolerance in agronomy.


2019 ◽  
Vol 476 (21) ◽  
pp. 3141-3159 ◽  
Author(s):  
Meiru Si ◽  
Can Chen ◽  
Zengfan Wei ◽  
Zhijin Gong ◽  
GuiZhi Li ◽  
...  

Abstract MarR (multiple antibiotic resistance regulator) proteins are a family of transcriptional regulators that is prevalent in Corynebacterium glutamicum. Understanding the physiological and biochemical function of MarR homologs in C. glutamicum has focused on cysteine oxidation-based redox-sensing and substrate metabolism-involving regulators. In this study, we characterized the stress-related ligand-binding functions of the C. glutamicum MarR-type regulator CarR (C. glutamicum antibiotic-responding regulator). We demonstrate that CarR negatively regulates the expression of the carR (ncgl2886)–uspA (ncgl2887) operon and the adjacent, oppositely oriented gene ncgl2885, encoding the hypothetical deacylase DecE. We also show that CarR directly activates transcription of the ncgl2882–ncgl2884 operon, encoding the peptidoglycan synthesis operon (PSO) located upstream of carR in the opposite orientation. The addition of stress-associated ligands such as penicillin and streptomycin induced carR, uspA, decE, and PSO expression in vivo, as well as attenuated binding of CarR to operator DNA in vitro. Importantly, stress response-induced up-regulation of carR, uspA, and PSO gene expression correlated with cell resistance to β-lactam antibiotics and aromatic compounds. Six highly conserved residues in CarR were found to strongly influence its ligand binding and transcriptional regulatory properties. Collectively, the results indicate that the ligand binding of CarR induces its dissociation from the carR–uspA promoter to derepress carR and uspA transcription. Ligand-free CarR also activates PSO expression, which in turn contributes to C. glutamicum stress resistance. The outcomes indicate that the stress response mechanism of CarR in C. glutamicum occurs via ligand-induced conformational changes to the protein, not via cysteine oxidation-based thiol modifications.


1974 ◽  
Vol 63 (1) ◽  
pp. 117-124 ◽  
Author(s):  
J. L. H. O'RIORDAN ◽  
J. S. WOODHEAD ◽  
G. N. HENDY ◽  
J. A. PARSONS ◽  
C. J. ROBINSON ◽  
...  

SUMMARY The presence of a single methionine in porcine parathyroid hormone, at position 8, permitted assessment of the role of this residue separate from the second methionine residue found at position 18 of bovine and human parathyroid hormones. Oxidation of the solitary methionine of porcine parathyroid hormone to the sulphoxide destroyed biological activity, but this was restored by subsequent reduction with cysteine. Oxidation of the hormone did not, however, affect its immunological activity; therefore, oxidation of the hormone may bring about dissociation of biological and immunological activity.


2012 ◽  
Vol 53 ◽  
pp. S137-S138
Author(s):  
Shibani Ratnayake ◽  
Shibani Ratnayake ◽  
Christopher Dunston ◽  
Eric Lattmann ◽  
Helen Griffiths

1956 ◽  
Vol 21 (1) ◽  
pp. 173-174 ◽  
Author(s):  
Irwin Fridovich ◽  
Philip Handler
Keyword(s):  

2019 ◽  
Vol 6 (4) ◽  
pp. 1009-1013 ◽  
Author(s):  
André H. B. Dourado ◽  
Matthias Arenz ◽  
Susana I. Córdoba de Torresi
Keyword(s):  

1981 ◽  
Vol 36 (3) ◽  
pp. 370-374 ◽  
Author(s):  
Shinji Ohmori ◽  
Kazuko Takahashi ◽  
Mikiko Ikeda ◽  
Toshihiko Ubuka

Abstract The desulfurization of several naturally occurring sulfur-containing amino acids by Raney nickel was studied under various conditions. Raney nickel, which was prepared by treating Al-Ni alloy with 5 N NaOH at 60 °C for 30 min, and was not washed with water, was most active and desulfurized, in quantitative yield, methionine, homocysteine, homocystine, homocysteine sulfinic acid, S-(2-carboxy-n-propyl)-L-cysteine, cysteine, cystine, cysteine sulfinic acid and S-methylcysteine sulfoxide. Raney nickel prepared from 100 mg of Al-Ni alloy desulfurized quantitatively up to 40 μmol methionine at 60 °C for 30 min. The desulfurization occurred effectively in the pH range of 7 and 13, but not below 7. Methionine sulfone, cysteic acid, and homocysteic acid were not subject to the reaction. The Raney nickel was deactivated by H2S, and H2O2, or combustion. Desulfurization activity was not enhanced by hydrogen gas.


2018 ◽  
Vol 14 (11) ◽  
pp. 991-993 ◽  
Author(s):  
Sophie Rahuel-Clermont ◽  
Michel B. Toledano
Keyword(s):  

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