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Related Concept Videos

Nucleotide Excision Repair01:38

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DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Updated: Aug 29, 2025

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
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RUP2 facilitates UVR8 redimerization via two interfaces.

Lixia Wang1, Yidong Wang1, Hongfei Chang1

  • 1National Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan 430070, China.

Plant Communications
|September 6, 2022
PubMed
Summary
This summary is machine-generated.

The plant UV RESISTANCE LOCUS 8 (UVR8) protein

Keywords:
COP1RUP2UV-B photoreceptorUVR8photomorphogenesis

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Area of Science:

  • Plant molecular biology
  • Photobiology
  • Structural biology

Background:

  • The UV RESISTANCE LOCUS 8 (UVR8) protein is a key photoreceptor mediating plant responses to UV-B radiation.
  • UVR8 functions by monomerizing upon UV-B perception and interacting with downstream signaling components.
  • REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins, RUP1 and RUP2, are known to facilitate the reversion of UVR8 to its inactive dimeric state.

Purpose of the Study:

  • To elucidate the structural basis of RUP2-mediated UVR8 redimerization.
  • To investigate the functional significance of different interaction interfaces between RUP2 and UVR8.
  • To understand the molecular mechanisms underlying UVR8 photocycle regulation.

Main Methods:

  • In vitro reconstitution of the RUP2-UVR8 complex.
  • X-ray crystallography to determine the complex structure at 2.0 Å resolution.
  • Biochemical assays and analysis of Arabidopsis thaliana mutants to assess functional impact.

Main Results:

  • The RUP2-UVR8 heterodimerization occurs through two distinct interfaces: the previously known Interface 1 and a newly identified Interface 2.
  • Interface 2 involves interactions between the RUP2 WD40 domain and the UVR8 core domain.
  • Disruption of Interface 2 significantly impaired UV-B induced photomorphogenic development in Arabidopsis.

Conclusions:

  • Both RUP2 and COP1 utilize a two-interface interaction mode with UVR8.
  • The identified RUP2-UVR8 interfaces are crucial for RUP2's role in facilitating UVR8 redimerization.
  • This study advances the understanding of the molecular interactions governing UVR8 photocycle regulation.