Methionine oxidation and reduction in proteins

Kim, Geumsoo; Weiss, Stephen J.; Levine, Rodney L.

doi:10.1016/j.bbagen.2013.04.038

Cited by 249 publications

(187 citation statements)

References 66 publications

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“…In addition, methionine, in contrast to isoleucine, is a sulfur-containing amino acid. Like the other sulfur-containing amino acid, cysteine, methionine residues can serve as cellular antioxidants, stabilize protein structure and act as regulatory switches through reversible oxidation and reduction [54]. It would, therefore, be very interesting to score the long-term survival phenotypes of our populations differing in ATPase6 in the presence and absence of an oxidative challenge.…”

Section: Discussionmentioning

confidence: 99%

The Cytoplasm Affects the Epigenome in Drosophila melanogaster

et al. 2018

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Cytoplasmic components and their interactions with the nuclear genome may mediate patterns of phenotypic expression to form a joint inheritance system. However, proximate mechanisms underpinning these interactions remain elusive. To independently assess nuclear genetic and epigenetic cytoplasmic effects, we created a full-factorial design in which representative cytoplasms and nuclear backgrounds from each of two geographically disjunct populations of Drosophila melanogaster were matched together in all four possible combinations. To capture slowly-accumulating epimutations in addition to immediately occurring ones, these constructed populations were examined one year later. We found the K4 methylation of histone H3, H3K4me3, an epigenetic marker associated with transcription start-sites had diverged across different cytoplasms. The loci concerned mainly related to metabolism, mitochondrial function, and reproduction. We found little overlap (<8%) in sites that varied genetically and epigenetically, suggesting that epigenetic changes have diverged independently from any cis-regulatory sequence changes. These results are the first to show cytoplasm-specific effects on patterns of nuclear histone methylation. Our results highlight that experimental nuclear-cytoplasm mismatch may be used to provide a platform to identify epigenetic candidate loci to study the molecular mechanisms of cyto-nuclear interactions.

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Section: Discussionmentioning

confidence: 99%

The Cytoplasm Affects the Epigenome in Drosophila melanogaster

et al. 2018

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“…The underlying molecular mechanisms that explain changes in protein function directly caused by Met oxidation have been previously reviewed (e.g., Levine et al 2000;Drazic and Winter 2014;Kim et al 2014a), and will only be addressed briefly herein. Apart from a general antioxidant role, Met functions through an oxidation/reduction cycle (Levine et al 1996(Levine et al , 2000Stadtman et al 2002).…”

Section: Met Oxidation Can Directly Regulate Protein Functionmentioning

confidence: 99%

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Rao

Thelen

Miernyk

2015

Cell Stress and Chaperones

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Oxidation of methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible posttranslational modification. It has been presumed that the major functional role for oxidation-labile Met residues is to protect proteins/ cells from oxidative stress. However, Met oxidation has been established as a key mechanism for direct regulation of a wide range of protein functions and cellular processes. Furthermore, recent reports suggest an interaction between Met oxidation and O-phosphorylation. Such interactions are a potentially direct interface between redox sensing and signaling, and cellular protein kinase/phosphatase-based signaling. Herein, we describe the current state of Met oxidation research, provide some mechanistic insight into crosstalk between these two major posttranslational modifications, and consider the evolutionary significance and regulatory potential of this crosstalk.

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“…HOCl-mediated oxidation of six identified Met residues in H. pylori KatA leads to methionine sulfoxide formation (Met-O), 2 protein oligomerization, and loss of catalase activity (3). Most organisms, including Helicobacter, possess a peptide repair enzyme, methionine sulfoxide reductase (Msr), that reduces Met-O back to Met in certain oxidation-susceptible Msr-targeted proteins (5,6). This Msr-mediated repair (along with added GroEL/ES) returns most of the catalase activity (3).…”

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confidence: 99%

Helicobacter Catalase Devoid of Catalytic Activity Protects the Bacterium against Oxidative Stress

Benoit

Maier

2016

Journal of Biological Chemistry

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Catalase, a conserved and abundant enzyme found in all domains of life, dissipates the oxidant hydrogen peroxide (H 2 O 2 ). The gastric pathogen Helicobacter pylori undergoes host-mediated oxidant stress exposure, and its catalase contains oxidizable methionine (Met) residues. We hypothesized catalase may play a large stress-combating role independent of its classical catalytic one, namely quenching harmful oxidants through its recyclable Met residues, resulting in oxidant protection to the bacterium. Two Helicobacter mutant strains (katA H56A and katA Y339A ) containing catalase without enzyme activity but that retain all Met residues were created. These strains were much more resistant to oxidants than a catalasedeletion mutant strain. The quenching ability of the altered versions was shown, whereby oxidant-stressed (HOCl-exposed) Helicobacter retained viability even upon extracellular addition of the inactive versions of catalase, in contrast to cells receiving HOCl alone. The importance of the methionine-mediated quenching to the pathogen residing in the oxidant-rich gastric mucus was studied. In contrast to a catalase-null strain, both site-change mutants proficiently colonized the murine gastric mucosa, suggesting that the amino acid composition-dependent oxidant-quenching role of catalase is more important than the well described H 2 O 2 -dissipating catalytic role. Over 100 years after the discovery of catalase, these findings reveal a new nonenzymatic protective mechanism of action for the ubiquitous enzyme.Catalase was described over 100 years ago (1), and the enzyme's role clearly is to detoxify H 2 O 2 by converting it into H 2 O and O 2 . It is one of he most abundant proteins in cells, and it is present in most organisms, including in both plant and animal cells (2). It is oftentimes a highly expressed protein. For example, in the gastric pathogen Helicobacter pylori, catalase (KatA) levels are estimated to be 4 -5% of the total protein content (3), and the katA gene is one of the most highly expressed genes in H. pylori cells recovered from the human stomach (4). HOCl-mediated oxidation of six identified Met residues in H. pylori KatA leads to methionine sulfoxide formation (Met-O), 2 protein oligomerization, and loss of catalase activity (3). Most organisms, including Helicobacter, possess a peptide repair enzyme, methionine sulfoxide reductase (Msr), that reduces Met-O back to Met in certain oxidation-susceptible Msr-targeted proteins (5, 6). This Msr-mediated repair (along with added GroEL/ES) returns most of the catalase activity (3). Although the identified protein targets of repair are few among the total of all organisms, some of these repair targets are themselves stress-combating enzymes.Purified KatA and Msr enzymes were shown to physically interact (6), and this interaction resulted in Msr-mediated repair of five out of the six oxidized KatA Met residues (3). In addition, H. pylori KatA is ubiquitous, present in both the cytoplasm and in the periplasm and on the cell surface as well as...

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Methionine oxidation and reduction in proteins

Cited by 249 publications

References 66 publications

The Cytoplasm Affects the Epigenome in Drosophila melanogaster

The Cytoplasm Affects the Epigenome in Drosophila melanogaster

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Helicobacter Catalase Devoid of Catalytic Activity Protects the Bacterium against Oxidative Stress

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