Rhee Sue Goo, Woo Hyun Ae
Yonsei Biomedical Research Institute, Yonsei University College of Medicine, Seoul, 120-749, South Korea; The Biochemistry and Biophysics Center, NHLBI, National Institutes of Health, Bethesda, MD, 20892, USA.
College of Pharmacy and College of Natural Sciences, Ewha Womans University, Seoul, 120-750, South Korea.
Free Radic Biol Med. 2020 May 20;152:107-115. doi: 10.1016/j.freeradbiomed.2020.02.028. Epub 2020 Mar 7.
Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for HO and rely on a conserved cysteine residue for rapid reaction with HO. Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of HO at specific area of the cells as well as sense and transduce HO signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys; phosphorylated on Ser, Thr, and Tyr; acetylated on Lys, Lys, Lys, Lys, and Lys; glutathionylated on Cys, Cys, and Cys; and nitrosylated on Cys and Cys, whereas Prx II is hyperoxidized on Cys; phosphorylated on Thr, Ser, and Thr; acetylated on Ala and Lys; glutathionylated on Cys and Cys; and nitrosylated on Cys and Cys. In this review, we describe how these post-translational modifications affect various functions of Prx I and Prx II.
过氧化物酶（Prxs）是一类特殊的硫醇特异性过氧化物酶家族，它们具有一个与过氧化氢（HO）结合的位点，并依靠一个保守的半胱氨酸残基与HO快速反应。在6种哺乳动物同工型（Prx I至VI）中，Prx I和Prx II主要存在于细胞质和细胞核中。在氧化应激条件下，Prx I和Prx II作为抗氧化酶和蛋白质伴侣发挥作用。在氧化正常应激条件下，Prx I和Prx II调节细胞特定区域的HO水平，并感知和转导HO信号至靶蛋白。已知Prx I和Prx II在多个位点发生共价修饰：Prx I在半胱氨酸上发生过氧化；在丝氨酸、苏氨酸和酪氨酸上发生磷酸化；在赖氨酸、赖氨酸、赖氨酸、赖氨酸和赖氨酸上发生乙酰化；在半胱氨酸、半胱氨酸和半胱氨酸上发生谷胱甘肽化；在半胱氨酸和半胱氨酸上发生亚硝基化，而Prx II在半胱氨酸上发生过氧化；在苏氨酸、丝氨酸和苏氨酸上发生磷酸化；在丙氨酸和赖氨酸上发生乙酰化；在半胱氨酸和半胱氨酸上发生谷胱甘肽化；在半胱氨酸和半胱氨酸上发生亚硝基化。在本综述中，我们描述了这些翻译后修饰如何影响Prx I和Prx II的各种功能。
