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

Ribosomes01:27

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Ribozymes02:47

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can be...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Ribosomes01:27

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...

You might also read

Related Articles

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

Sort by
Same author

The morphology of internal elastic lamina corrugations in arteries under physiological conditions.

Morphologie : bulletin de l'Association des anatomistes·2024
Same author

Adaptive Remodeling in the Elastase-induced Rabbit Aneurysms.

Experimental mechanics·2021
Same author

Regional patterns of nuptiality in Europe, 1870-1960.

Population studies·2011
Same author

Multiphoton intravital microscopy of the transplanted mouse kidney.

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons·2011
Same author

Metastasis-associated phosphatase PRL-2 regulates tumor cell migration and invasion.

Oncogene·2011
Same author

Anti-Amyloid Effects of Small Molecule Aβ-Binding Agents in PS1/APP Mice.

Letters in drug design & discovery·2010

Related Experiment Video

Updated: Jun 28, 2026

Induction of Mouse Lung Injury by Endotracheal Injection of Bleomycin
06:52

Induction of Mouse Lung Injury by Endotracheal Injection of Bleomycin

Published on: April 30, 2019

Human bleomycin hydrolase binds ribosomal proteins.

R P Koldamova1, I M Lefterov, M T DiSabella

  • 1Department of Pharmacology, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.

Biochemistry
|June 3, 1999
PubMed
Summary

Human bleomycin hydrolase (hBH), an enzyme that inactivates the anticancer drug bleomycin, interacts with ribosomal proteins. This study reveals hBH

More Related Videos

A Mouse Model of Pulmonary Fibrosis Induced by Nasal Bleomycin Nebulization
02:46

A Mouse Model of Pulmonary Fibrosis Induced by Nasal Bleomycin Nebulization

Published on: January 20, 2023

Oropharyngeal Administration of Bleomycin in the Murine Model of Pulmonary Fibrosis
06:03

Oropharyngeal Administration of Bleomycin in the Murine Model of Pulmonary Fibrosis

Published on: May 9, 2025

Related Experiment Videos

Last Updated: Jun 28, 2026

Induction of Mouse Lung Injury by Endotracheal Injection of Bleomycin
06:52

Induction of Mouse Lung Injury by Endotracheal Injection of Bleomycin

Published on: April 30, 2019

A Mouse Model of Pulmonary Fibrosis Induced by Nasal Bleomycin Nebulization
02:46

A Mouse Model of Pulmonary Fibrosis Induced by Nasal Bleomycin Nebulization

Published on: January 20, 2023

Oropharyngeal Administration of Bleomycin in the Murine Model of Pulmonary Fibrosis
06:03

Oropharyngeal Administration of Bleomycin in the Murine Model of Pulmonary Fibrosis

Published on: May 9, 2025

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Bleomycin hydrolase (BH) is a cysteine proteinase crucial for inactivating the anticancer drug bleomycin.
  • Yeast BH exhibits a homohexameric structure akin to a 20S proteasome, with known binding to single-stranded RNA and DNA.

Purpose of the Study:

  • To investigate the cellular localization and binding partners of human bleomycin hydrolase (hBH).
  • To determine if hBH interacts with ribosomal proteins and identify its subcellular location.

Main Methods:

  • Yeast two-hybrid system to identify hBH binding partners.
  • In vitro co-precipitation assays using 35S-labeled proteins.
  • Immunofluorescence microscopy to confirm colocalization.
  • Differential centrifugation and Western immunoblotting to analyze subcellular fractions.
  • In vitro binding assays with microsomes.

Main Results:

  • Human BH (hBH) was found to interact with and colocalize with ribosomal proteins L11 and L29.
  • The N-terminus of hBH, including the catalytic Cys93, was essential for binding to L11.
  • hBH activity and the protein itself were detected in the ribosomal subcellular fraction.
  • Recombinant hBH demonstrated binding to microsomes in vitro.

Conclusions:

  • Human BH (hBH) functions not only as a free cytosolic enzyme but also associates with ribosomes.
  • These findings suggest a novel role for hBH in ribosome-associated cellular processes.