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Related Concept Videos

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
RNA Structure01:19

RNA Structure

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.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
RNA Structure01:23

RNA Structure

Overview
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.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA): messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three RNA types consist of a...

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Related Experiment Video

Updated: Jun 20, 2026

Chemical Triphosphorylation of Oligonucleotides
13:19

Chemical Triphosphorylation of Oligonucleotides

Published on: June 2, 2022

Structure-activity relationships in human RNA 3'-phosphate cyclase.

Naoko Tanaka1, Stewart Shuman

  • 1Sloan-Kettering Institute, New York, New York 10065, USA.

RNA (New York, N.Y.)
|August 20, 2009
PubMed
Summary

RNA 3'-phosphate cyclase (Rtc) enzymes create RNA 2',3' cyclic phosphate ends. Key residues in human Rtc1 were identified through structural analysis, revealing their essential roles in RNA cyclization and binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • RNA 3 -phosphate cyclase (Rtc) enzymes synthesize RNA 2 ,3 cyclic phosphate ends.
  • This process involves a three-step ATP-dependent nucleotidyl transfer mechanism.

Purpose of the Study:

  • To elucidate the structure-activity relationships of human RNA cyclase Rtc1.
  • To identify essential residues for RNA cyclization and autoadenylation reactions.

Main Methods:

  • Utilized the crystal structure of Escherichia coli RtcA to guide mutational analysis of human Rtc1.
  • Performed alanine scanning and conservative substitutions to assess residue function.
  • Investigated RNA 3 -phosphate and 3 -OH terminated RNA binding.

Main Results:

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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

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Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates
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Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates

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Last Updated: Jun 20, 2026

Chemical Triphosphorylation of Oligonucleotides
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Chemical Triphosphorylation of Oligonucleotides

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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro
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Analysis of RNA Processing Reactions Using Cell Free Systems: 3' End Cleavage of Pre-mRNA Substrates in vitro

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Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates
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Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates

Published on: May 8, 2020

  • Identified seven conserved residues essential for Rtc1 RNA cyclization and autoadenylation.
  • Proposed a mechanism for adenylate transfer involving specific residue interactions (His320, Arg21, Arg40, Arg43, Tyr294, Glu14).
  • Demonstrated that Rtc1 binds 3 -phosphate terminated RNA but not 3 -OH terminated RNA, and His320 mutation does not affect RNA binding.

Conclusions:

  • Seven conserved residues are critical for human Rtc1 enzyme function.
  • Specific residues facilitate ATP binding and adenylate transfer.
  • RNA 3 -phosphate recognition by Rtc1 is independent of its adenylylation state.