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Related Concept Videos

Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
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RNA Structure01:19

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The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Bacterial Transcription01:53

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RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
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Restarting Stalled Replication Forks02:37

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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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Related Experiment Video

Updated: Dec 12, 2025

Estimation of Telomeric Repeat-containing RNA from DNA/RNA Hybrid Complexes
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Estimation of Telomeric Repeat-containing RNA from DNA/RNA Hybrid Complexes

Published on: December 5, 2025

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Replication protein A binds RNA and promotes R-loop formation.

Olga M Mazina1, Srinivas Somarowthu1, Lyudmila Y Kadyrova2

  • 1Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania, USA.

The Journal of Biological Chemistry
|August 16, 2020
PubMed
Summary

Replication protein A (RPA) binds RNA with high affinity, revealing its role in RNA metabolism and R-loop formation. This finding suggests a new mechanism for genome maintenance and DNA replication restart.

Keywords:
DNA polymeraseDNA repairDNA replicationDNA replication restartR-loop extensionR-loopsRNARNA-binding proteinhomologous recombination

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Replication protein A (RPA) is a key eukaryotic protein binding single-stranded DNA (ssDNA).
  • RPA is crucial for DNA replication, repair, and damage signaling.
  • RPA was thought to bind RNA weakly, but emerging evidence suggests a role in RNA metabolism.

Purpose of the Study:

  • To investigate the RNA-binding properties of human RPA.
  • To explore RPA's potential role in R-loop formation.

Main Methods:

  • Gel-retardation assays to assess RPA-RNA binding affinity.
  • RNA/DNA competition assays to quantify binding specificity.
  • Reconstitution experiments with human DNA polymerases.

Main Results:

  • Human RPA binds RNA with high affinity (Kd ≈ 100 pM).
  • RPA binding to RNA promotes R-loop formation with double-stranded DNA.
  • RPA-generated R-loops can initiate DNA synthesis by human DNA polymerases.

Conclusions:

  • RPA exhibits significant RNA-binding capabilities, expanding its known functions beyond ssDNA binding.
  • RPA actively participates in RNA metabolism and R-loop formation.
  • RPA-mediated R-loop formation provides a mechanism for replication restart and genome maintenance.