Related Experiment Video
Updated: Jun 4, 2025

10:38
Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli
Published on: November 30, 2018
9.6K
DNA Ligase I Circularises Potato Spindle Tuber Viroid RNA in a Biomolecular Condensate
Yunhan Wang1, Junfei Ma2, Jie Hao2
1Plant Molecular and Cell Biology Program, University of Florida, Gainesville, Florida, USA.
Molecular Plant Pathology
|December 23, 2024
Summary
Viroids are plant pathogens that replicate in the nucleus. This study reveals potato spindle tuber viroid RNA and DNA ligase I form a biomolecular condensate near the nucleolus for RNA processing.
Area of Science:
- Molecular Biology
- Plant Pathology
- Virology
Background:
- Viroids are small, circular, noncoding RNA pathogens infecting plants.
- Nuclear replication involves host RNA polymerase II and protein TFIIIA-7ZF.
- Differential localization of RNA strands and the ligation step remain unclear.
Purpose of the Study:
- To investigate the subcellular localization and function of DNA ligase I (LIG1) during viroid replication.
- To elucidate the mechanism of circular RNA progeny formation.
- To understand the role of biomolecular condensates in subviral pathogen infection.
Main Methods:
- Confocal microscopy to observe colocalization of LIG1 and PSTVd RNA in Nicotiana benthamiana protoplasts.
- Analysis of RNA condensation and its association with LIG1.
- Investigating the role of biomolecular condensates in viroid RNA processing.
Main Results:
- Potato spindle tuber viroid (PSTVd) RNA and LIG1 colocalize near the nucleolar region.
- This colocalized region represents a condensed state of PSTVd RNA.
- Evidence suggests PSTVd RNA and LIG1 form a biomolecular condensate for RNA processing.
Conclusions:
- Viroid RNA processing and ligation occur within a biomolecular condensate near the nucleolus.
- This finding expands the known functions of biomolecular condensates to include subviral pathogen interactions.
- Understanding viroid biogenesis aids in studying newly identified viroid-like RNAs.
Related Concept Videos
Translesion DNA Polymerases
9.8K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
9.8K
Nucleic Acid Structure
5.9K
The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms a 5′ to 3′ phosphodiester linkage.
DNA Structure
DNA...
DNA Structure
DNA...
5.9K
Homologous Recombination
50.2K
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...
50.2K
Protein Complex Assembly
10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K
Restarting Stalled Replication Forks
5.7K
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,...
5.7K
The Replisome
33.0K
DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
33.0K

