Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Transcription Attenuation in Prokaryotes02:42

Transcription Attenuation in Prokaryotes

Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
Transfer RNA Synthesis02:36

Transfer RNA Synthesis

One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
Each of these chemical modifications is carried by a specific enzyme, post-transcription. All of these enzymes have unique base and site-specificity. Methylation, the most common chemical modification, is carried by at least nine different enzymes, with...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Internal in-frame translation generates Cas11b, which is important for effective interference in an archaeal CRISPR-Cas system.

Frontiers in microbiology·2025
Same author

Practical laboratory class to assess gene silencing using CRISPR interference (CRISPRi) technology in the archaeon Haloferax volcanii.

Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology·2024
Same author

17q21 variant increases the risk of exacerbations in asthmatic children despite inhaled corticosteroids use.

Allergy·2018
Same author

Expression and release of platelet protein disulphide isomerase in patients with haemophilia A.

Haemophilia : the official journal of the World Federation of Hemophilia·2016
Same author

Relevant bleeding diathesis due to acquired factor XIII deficiency.

Hamostaseologie·2013
Same author

Medication safety improves after implementation of positive patient identification.

Applied clinical informatics·2013

Related Experiment Video

Updated: Jul 14, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase
09:25

In vitro Reconstitution of the Active T. castaneum Telomerase

Published on: July 14, 2011

tRNase Z: the end is not in sight.

B Späth1, G Canino, A Marchfelder

  • 1Molekulare Botanik, Universität Ulm, Albert-Einstein-Allee 11, 89069, Ulm, Germany.

Cellular and Molecular Life Sciences : CMLS
|June 30, 2007
PubMed
Summary

tRNase Z is an endonuclease that processes tRNA 3' ends. This review covers its substrates, pre-tRNA and bpNPP, and metal requirements for enzyme function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • tRNase Z is an endonuclease crucial for tRNA maturation.
  • It removes the tRNA 3' trailer, preparing the 3' end for CCA addition and aminoacylation.
  • The enzyme also cleaves bis(p-nitrophenyl)phosphate (bpNPP), its smallest known substrate.

Purpose of the Study:

  • To review current knowledge on tRNase Z.
  • To summarize information on tRNase Z substrates: pre-tRNA and bpNPP.
  • To discuss the metal ion requirements for tRNase Z activity.

Main Methods:

  • Literature review of existing studies on tRNase Z.
  • Analysis of biochemical data concerning tRNase Z activity.
  • Compilation of information on substrate interactions and metal ion dependencies.

More Related Videos

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on (TRO) Approach
12:12

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on (TRO) Approach

Published on: March 12, 2017

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 (Ehmeth) Enzyme
12:36

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 (Ehmeth) Enzyme

Published on: October 19, 2010

Related Experiment Videos

Last Updated: Jul 14, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase
09:25

In vitro Reconstitution of the Active T. castaneum Telomerase

Published on: July 14, 2011

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on (TRO) Approach
12:12

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on (TRO) Approach

Published on: March 12, 2017

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 (Ehmeth) Enzyme
12:36

In vitro tRNA Methylation Assay with the Entamoeba histolytica DNA and tRNA Methyltransferase Dnmt2 (Ehmeth) Enzyme

Published on: October 19, 2010

Main Results:

  • tRNase Z has a defined role in tRNA 3' end processing.
  • bpNPP represents the smallest characterized substrate for tRNase Z.
  • Biological functions of tRNase Z have been identified in both prokaryotic and eukaryotic organisms.
  • Specific metal ions are essential for tRNase Z enzymatic activity.

Conclusions:

  • tRNase Z is a key enzyme in tRNA processing with diverse substrates.
  • Understanding its metal requirements is vital for elucidating its catalytic mechanisms.
  • Further research is needed to fully characterize tRNase Z across different species.