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Related Concept Videos

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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. 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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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
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Nucleic Acid Structure01:25

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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.
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Homologous Recombination02:31

Homologous Recombination

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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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Related Experiment Video

Updated: Nov 9, 2025

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

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Mtr4 RNA helicase structures and interactions.

Keith J Olsen1, Sean J Johnson1

  • 1Department of Chemistry and Biochemistry, Utah State University, Logan, UT84322-0300, USA.

Biological Chemistry
|April 15, 2021
PubMed
Summary
This summary is machine-generated.

Mtr4, an RNA helicase, activates the RNA exosome for RNA surveillance. Recent structural studies reveal its role in recruiting RNA substrates, but gaps in understanding remain.

Keywords:
Mtr4RNA helicaseRNA surveillanceSki2-like helicasestructure

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Mtr4 is a Ski2-like RNA helicase crucial for RNA surveillance and degradation.
  • It functions as an activator of the RNA exosome complex.
  • RNA helicases play vital roles in cellular RNA metabolism and gene regulation.

Purpose of the Study:

  • To review and summarize the structural insights into Mtr4.
  • To highlight Mtr4's interactions with protein and nucleic acid partners.
  • To identify current gaps in the understanding of Mtr4 structure and function.

Main Methods:

  • Review of multiple crystallographic and cryo-electron microscopy (cryo-EM) studies.
  • Analysis of structural data to understand Mtr4's mechanism.
  • Integration of structural findings with biochemical and genetic data.

Main Results:

  • Structural studies over the past decade have elucidated Mtr4's molecular architecture.
  • Mtr4 is positioned centrally in a dynamic complex that binds and presents RNA substrates.
  • Key interactions with protein partners and nucleic acids have been characterized.

Conclusions:

  • Structural data provides a dynamic view of Mtr4's role in RNA processing.
  • Further research is needed to address the identified gaps in Mtr4's functional mechanism.
  • Understanding Mtr4 structure is key to deciphering RNA surveillance pathways.