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Updated: Jun 23, 2026

Immunofluorescence Imaging of DNA Damage and Repair Foci in Human Colon Cancer Cells
Published on: June 9, 2020
RecX is involved in the switch between DNA damage response and normal metabolism in D. radiodurans
Duohong Sheng1, Jiandong Jao, Mingfeng Li
1State Key Laboratory of Microbial Technology, Shandong University, 250100 Jinan, China. dhsheng@sdu.edu.cn
Abstract:
Apart from inhibiting RecA activity through protein-protein interactions, Deinococcus radiodurans RecX inhibits the expression of RecA and two other anti-oxidant proteins. To identify the repertoire of proteins regulated by RecX, comparative proteomic studies were undertaken on a wild-type strain (R1) and recX null mutant (RecX(-)). Two-dimensional electrophoresis followed by MALDI-TOF identification revealed 35 differentially expressed proteins, including 12 up-regulated and 23 down-regulated proteins in the mutant. The 12 up-regulated proteins are DNA repair proteins, stress response proteins, and metabolism-related proteins. Most of these have been previously characterized as ionizing radiation-induced proteins. The 23 down-regulated proteins are mainly involved in cellular metabolism, and some of these are key enzymes in the metabolic pathway. Thus, RecX is suggested to be involved in the switch between DNA damage response and normal metabolism in D. radiodurans.
Insights
Deinococcus radiodurans RecX regulates DNA repair and metabolism proteins. Proteomic analysis revealed RecX controls 35 differentially expressed proteins, impacting DNA damage response and cellular metabolism.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Deinococcus radiodurans possesses remarkable radiation resistance.
- RecX protein is known to inhibit RecA activity via protein-protein interactions.
- RecX also downregulates the expression of RecA and antioxidant proteins.
Purpose of the Study:
- To comprehensively identify all proteins regulated by RecX in D. radiodurans.
- To understand the role of RecX in coordinating DNA damage response and metabolic processes.
Main Methods:
- Comparative proteomic analysis using two-dimensional electrophoresis.
- Protein identification via Matrix-Assisted Laser Desorption/Ionization-Time of Flight (MALDI-TOF) mass spectrometry.
- Comparison between wild-type (R1) and recX null mutant (RecX(-)) strains.
Main Results:
- 35 differentially expressed proteins were identified between wild-type and recX mutant strains.
- 12 proteins were upregulated in the recX mutant, including DNA repair, stress response, and metabolism proteins.
- 23 proteins were downregulated in the recX mutant, primarily involved in cellular metabolism, including key metabolic enzymes.
Conclusions:
- RecX regulates a broad repertoire of proteins beyond its known interaction with RecA.
- RecX plays a crucial role in modulating the switch between DNA damage response pathways and normal cellular metabolism in D. radiodurans.
- The findings suggest RecX acts as a central regulator integrating environmental stress responses with metabolic status.
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