Reactive Oxygen Species and Cellular Function Switch

Seong Eon Ryu

doi:10.7599/hmr.2013.33.2.104

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Ryu: Reactive Oxygen Species and Cellular Function Switch

Review Article

Hanyang Medical Reviews 2013; 33(2): 104-109.

Published online: 23 May 2013

DOI: https://doi.org/10.7599/hmr.2013.33.2.104

Reactive Oxygen Species and Cellular Function Switch

Seong Eon Ryu

Department of Bioengineering, College of Engineering, Hanyang University, Seoul, Korea.

Correspondence to: Seong Eon Ryu. Department of Bioengineering, College of Engineering, Hanyang University, 222 Wangsimri-ro, Seongdong-gu, Seoul 133-791, Korea. Tel: +82-2-2220-4020, Fax: +82-2-2220-4023, ryuse@hanyang.ac.kr

Received 12 March 2013 Revised 22 April 2013 Accepted 25 April 2013

(open-access):

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Reactive oxygen species (ROS) are harmful to cellular components such as proteins, DNA and lipids. The continuous production of ROS during the respiratory electron transfer process has been regarded as the major cause of aging. However, the discoveries of proteins whose structure and function switch with cellular ROS suggest that ROS are active players in cellular regulation. OxyR is the first protein whose ROS-regulated mechanism was revealed by the atomic structure studies. The distantly-located two cysteines in OxyR form a disulfide bond by reaction with ROS, resulting in conformational and functional switches in the protein. The heat shock protein 33 is another protein that is activated by increased level of cellular ROS. Many other cellular proteins including protein tyrosine phosphatases are also regulated by ROS. This review focuses on the structure and function of the ROS-regulated proteins and their implications on the ROS's cellular roles. Detailed studies on the ROS-generating protein machinery and the ROS-regulated proteins should contribute to the therapeutic control of ROS-related diseases and aging processes.

Keywords: Reactive Oxygen Species, OxyR, Hsp33, Protein Tyrosine Phosphatase, Protein Structure

Figures and Tables

Fig. 1

ROS's cellular function regulation network. The mitochondria-derived ROS play two roles including cellular function regulation and promotion of diseases/aging. The cellular function regulation by ROS is likely to feedback its results to mitochondria, resulting in the control of ROS generation level. It will be necessary to understand the balance between the ROS's effects on diseases/aging and the cellular function regulation.

Fig. 2

ROS-mediated structural switch in OxyR. The reduced OxyR (left-hand side) has two cysteines (Cys199 and Cys208) that are distant to each other (the inter-sulfur atom distance: 17 Å). ROS oxidize the two cysteines, resulting in a disulfide bond of the oxidized OxyR (right-hand side). For the disulfide bond formation, two cysteines travel to a close location to each other, causing large structural transitions that affect the monomeric and dimeric interaction surfaces and promote the oxidized OxyR-mediated transcription of antioxidant proteins.

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