Trafficking of DNA Repair Factors Into Mitochondria for the Repair of Oxida- Tive Lesions on Mtdna

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Trafficking of DNA Repair Factors Into Mitochondria for the Repair of Oxida- Tive Lesions on Mtdna Central Journal of Pharmacology & Clinical Toxicology Review Article *Corresponding author Tikam Chand Dakal, Genome & Computational Biology Lab, Department of Biotechnology, Mohanlal Sukhadia Trafficking of DNA Repair University, Udaipur-313001, Rajasthan, India, Tel: 8107326969; Email: [email protected] Submitted: 18 December 2019 Factors into Mitochondria for Accepted: 04 January 2020 Published: 08 January 2020 the Repair of Oxidative Lesions ISSN: 2333-7079 Copyright on mtDNA © 2020 Dakal et al. OPEN ACCESS Tikam Chand Dakal1*, Bhanupriya Dhabhai1, Ramgopal Dhakar1, Athira M. Menon1, and Narendra K. Sharma2 Keywords 1Department of Biotechnology, Mohanlal Sukhadia University, India • APE1; Mitochondria; mtDNA; Oxidative damages; 2Department of Bioscience and Biotechnology, Banasthali Vidyapith University, India Tim40/MIA import pathway Abstract Cells become cancerous after being faced with several cellular insults, including DNA damages caused by oxidative stresses. Mitochondria are the main endogenous source of reactive oxygen species (ROS) because most ROS are generated by the oxidative phosphorylation processes that occur in mitochondria. ROS induce oxidative lesions and base alkylation in mtDNA that are thought to be repaired via BER pathway. However, the DNA repair proteins and other components/factors of BER pathway are not produced in the mitochondria but are translocated from cytoplasm or nucleus. This review explicitly presents the molecular, cellular and structural basis for trafficking of DNA repair proteins/factors, in particular APE1 from the cytoplasm to the mitochondria. INTRODUCTION C-terminus, which is masked by the NLS domain at N-terminal Alterations in DNA and protein sequences have a severe and regulated mechanisms of protein unfolding-refolding to implication in the development and progression of many ensure(residues proper 1-39), APE1 therefore localization. suggesting Deletion the occurrenceof the N-terminal of specific NLS diseases, such as cancers and neurodegenarative disorders [1- 7]. Apurinic/apyrimidinic endonuclease 1 (APE1) is an essential non-canonical subcellular compartments such as mitochondria protein that possesses DNA repair activity and redox activity. [11].(NΔ33) redirects the truncated protein (NΔ33 APE1) towards As such APE1 is known to interact with a number of proteins as presented in Figure 1 [8], and therefore, is implicated in a number of diseases (Figure 2 & 3) [9]. APE1 has a redox active Cysteine IL8 [12]. A novel APE1 interacting (Cys65) through which it maintains reduced state of several Researchers found that APE1 cause deregulated expression of a pro-inflammatory gene, p53. This reduced state is required for facilitating their binding partner, peroxiredoxine 1 (PRDX1), is involvedIL8. For in this, cellular reduction redox ontoredox-regulated the promoter transcription of the target factors, gene so such as to as turn AP-1, on theirNFκB gene and regulation. PRDX1 knockdown in HepG2 cells causes increased expression. The DNA repair and redox activities of APE1 reside inexpression the nucleus of a and pro-inflammatory in absence of thisgene, interaction (as in case of within distinct domains of the protein. APE1 is involved in the of cysteine in NFκB is required. APE1 interacts with PRDX1 base damage caused by various oxidative and alkylating agents, PRDX1 knockdown), APE1 interact NFκB and causes reduction base excision repair (BER) pathway, which repairs oxidative of its cysteine. PRDX1 interacts with APE1 in nucleus in such a includes four distinct steps: (i) recognition and removal of the way that PRDX1 sequesters APE1 redox activity, thereby keeps a check on APE1 from reducing NFκB. Based on results presented both of endogenous and exogenous nature. The BER pathway/ apyrimidinic (AP) sites; (ii) processing of the generated AP site by Cesaratto and Xie [13,14], from several such experiments bymodified APE1 protein;base by a(iii) DNA incorporation glycosylase andof the generation correct nucleotide(s) of apurinic for instance, ELISA assay, Western blots, Immunofluorescence microscopy, Microarray analysis, and qPCR, it can be interpreted catalyzed by the DNA ligase III. Although much is known that PRDX1 interaction with APE1 represents a cellular defensiveIL8 aboutthrough how the APE1activity proteins of the polymeraseare targeted γ; to and and (iv) imported nick sealing into expression,mechanism whichin which otherwise the APE1-PRDX1could increase interaction the susceptibility keeps ofa nucleus, very little is known about how APE1 gets targeted and check on APE1 redox activity from activating superfluous translocated into mitochondria and recruited to sites of DNA lesions. Li [10], demonstrated that the mitochondrial targeting pro-inflammatory response and cancer metastasis. signal (MTS) of APE1 resides within residues 289-318 of the PRDX1 knockdown or loss causes protein hyperoxidation in HepG2, HeLa cells, MDA-MB-231 and other cell lines [13,15]. PRDX1 interacts with RAD51 under oxidative conditions Cite this article: Dakal TC, Dhabhai B, Dhakar R, Menon AM, Sharma NK (2020) Trafficking of DNA Repair Factors into Mitochondria for the Repair of Oxida- tive Lesions on mtDNA. J Pharmacol Clin Toxicol 8(1):1137. Dakal et al. (2020) Central Figure 1 Experimentally verified interacting partners of APE1. Figure 2 The gene expression profile across all tumor samples and paired normal tissues represented in the form of a Dot Plot. Each dot represent expression of samples. and protects the functially important cys319 residue in can be easily detected and visualized by immunofluorescence RAD51 [14]. PRDX1 catalyzes the reduction of H2O2 into imaging with mitochondria specific red-fluorescent dye, such as H2O. The knockdown of PRDX1 is also expected to cause the MITOTRACKER. Besides this, PRDX1 knockdown, indeed, may hyperoxidation of cell organelles, especially mitochondria which cause upregulation of mitochondrial respiration and which in- J Pharmacol Clin Toxicol 8(1): 1137 (2020) 2/4 Dakal et al. (2020) Central CELLULAR AND MOLECULAR BASIS FOR APE1 TRAFFICKING Over 99% of proteins required for mitochondrial functioning are encoded by the nuclear genome [19,20], and transported into the mitochondria after synthesis in the cytosol. Such proteins use the TOM (translocase of outer mitochondrial membrane) and TIM (translocase of inner mitochondrial membrane) translocation machineries in the mitochondrial outer membrane (MOM) and MIM, respectively, for their transport into mitochondrial matrix Figure 3 [21]. APE1 is an essential component of the BER pathway in The gene expression profile across all tumor samples and mitochondria and is translocated from cytosol to mitochondria paired normal tissues represented in the form of a Bar plot in which using similar mechanism. Recently, Barchiesi [16], demonstrated the height of bar represents the median expression of certain tumor that APE1 interacts with the mitochondrial import and assembly type or normal tissue. protein Mia40 in the intermembrane space (IMS) and that suggested that Mia40 is responsible for APE1 trafficking into The precise mechanism of Apn1 sorting from the MIM to the matrix will be strong evidence for Apn1 possible role in DNA repair in the MIM. However, further translocation of APE1 from the MIM mitochondria, which will represent a novel pathway until now to the matrix is still not clear. The repair synthesis by APE1 is believed to be nonexistent. critical for maintenance of mitochondrial DNA stability and integrity because unrepaired mtDNA could potentially increase the susceptibility to mitochondrial and other diseases such as Apn1 interacts with proteins involved in oxidative balance and mitochondrial BER pathway such as DNA glycosylase, Polymerase cancer,APPROACH cardio-vascular, FOR TESTING and neuro-degenerative AND CONFIRM disorders. APE1 γ (POLG) and Ligase III. TRAFFICKING IN MITOCHONDRIA Saccharomyces Understanding in-depth mechanisms of Apn1-mediated maintenance cerevisiae of mtDNA integrity may provide targets for clinical interventions for APE1 has a yeast counterpart, Apn1, in prevention and treatment of human diseases mentioned above. which can be efficiently usedin forvitro elucidating the mechanism of Apn1 sorting from the IMS to the matrix for repairing lesions of mtDNA. For this, an import assays Identification of Apn1 interacting proteins & role in DNA repair is for radioisotope-labelled Apn1 need to establish. It would expected to evolve as a new area of research be essential to test and confirm that the Apn1 uses the MIA system to reach the IMS by using the mutants of Mia40 and Figure 4 Erv1 (Figure 4). Further, optimization of the assay condition to achieve efficient sorting of the Apn1 to the matrix, not the IMS Possible outcomes from the studies on APN1 trafficking in is required. There exists some translocators such as the TIM23 mitochondria. complex and TIM22 complex and their possible involvement in Apn1 trafficking in mitochondria is also required to be checked turn many elevates glucose uptake by the cells, both contributed by using their temperature-sensitive (ts) mutant mitochondria. to increased proliferation of PRDX1 knockdown cells as compared Test of requirement of energy like the membrane potential to wild-type cells indicating that PRDX1 knockdown may render across the IM and ATP hydrolysis by matrix Hsp70 can also be cellsAPE1 go cancerous.TRAFFICKING IN MITOCHONDRIA IS VIA checked. One can also use crosslinking approaches or affinity co- TIM, TOM AND MIA IMPORT PATHWAY
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