Lysines and cysteines: partners in stress?

Rabe von Pappenheim, Fabian; Tittmann, Kai

Rabe von Pappenheim, Fabian; Tittmann, Kai.

Afiliação

Rabe von Pappenheim F; Department of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg August University Göttingen, Julia-Lermontowa-Weg 3, D-37077 Göttingen, Germany; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. Electronic address: fpappen@gwdg.de.
Tittmann K; Department of Molecular Enzymology, Göttingen Center of Molecular Biosciences, Georg August University Göttingen, Julia-Lermontowa-Weg 3, D-37077 Göttingen, Germany; Department of Structural Dynamics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. Electronic address: ktittma@gwdg.de.

Trends Biochem Sci ; 47(5): 372-374, 2022 05.

Article em En | MEDLINE | ID: mdl-35427478

ABSTRACT

ABSTRACT

Modifications of cysteine residues in redox-sensitive proteins are key to redox signaling and stress response in all organisms. A novel type of redox switch was recently discovered that comprises lysine and cysteine residues covalently linked by an nitrogen-oxygen-sulfur (NOS) bridge. Here, we discuss chemical and biological implications of this discovery.

Assuntos

Cisteína; Lisina; Cisteína/química; Lisina/metabolismo; Oxirredução; Estresse Oxidativo; Processamento de Proteína Pós-Traducional; Proteínas/química

Palavras-chave

cysteine reactome; oxidative stress; post-translational modifications; redox biology

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Texto completo: 1 Bases de dados: MEDLINE Assunto principal: Cisteína / Lisina Idioma: En Revista: Trends Biochem Sci Ano de publicação: 2022 Tipo de documento: Article