NDLI: Thioredoxin-dependent redox regulation of cellular signaling and stress response through reversible oxidation of methionines

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Molecular BioSystems Vol - 7 Issue - 6

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Thioredoxin-dependent redox regulation of cellular signaling and stress response through reversible oxidation of methionines

Content Provider	Royal Society of Chemistry (RSC)
Author	Bigelow, Diana J. Squier, Thomas C.
Copyright Year	2011
Abstract	The sensitive oxidations of sulfur containing amino acids (i.e., cysteines and methionines) commonly control protein function, and act as important signaling mechanisms to modify metabolic responses to environmental stressors. Mechanisms associated with cysteine oxidation to form sulfenic acid and disulfides (i.e., cystine and glutathione adducts), and their reversibility through thioredoxin-dependent mechanisms, are broadly appreciated as important regulatory mechanisms that control the function of a range of different proteins. Less commonly understood are the cellular consequences of methionine oxidation to form methionine sulfoxide, as the structural requirements for their thioredoxin-dependent reduction by methionine sulfoxide reductases limit the reversibility of methionine oxidation to sequences within surface exposed and conformationally disordered regions of proteins. Surface exposed methionines are commonly involved in molecular recognition between transient protein signaling complexes, where their oxidation disrupts productive protein–protein interactions linked to a range of cellular responses. Such a signaling protein is calmodulin, which represents an early and central point in calcium signaling pathways important to stress responses in plants. We describe recent work elucidating fundamental mechanisms of reversible methionine oxidation within calmodulin, including the physical basis for differences in the sensitivity of individual methionines within plant and animal calmodulin to reactive oxygen species (ROS), the structural and functional consequences of their oxidation, and the interactions of oxidized calmodulin with methionine sulfoxide reductase enzymes. It is suggested that, in combination with high-throughput proteomic methods and current generation informatics tools, these mechanistic insights permit useful predictions of oxidatively sensitive signaling proteins that act as redox and stress sensors in response tomethionine oxidation.
Starting Page	2101
Ending Page	2109
Page Count	9
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	7
Journal	Molecular BioSystems
DOI	10.1039/c1mb05081h
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Calcium signaling Cysteine Reactive oxygen species Methionine sulfoxide Methionine Redox Protein Cystine Sulfoxide Sulfur Base pair Calmodulin Glutathione
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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