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

Bacterial Signaling01:30

Bacterial Signaling

40.3K
Bacterial signaling can occur within bacteria (intracellular) or between bacteria (intercellular). At times, a group of bacteria behaves like a community. To achieve this, they engage in quorum sensing, the perception of higher cell density that causes changes in gene expression. Quorum sensing involves both extracellular and intracellular signaling. The signaling cascade starts with a molecule called an autoinducer (AI). Individual bacteria produce AIs that move out of the bacterial cell...
40.3K
Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

616
Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a...
616
What is Cell Signaling?02:03

What is Cell Signaling?

129.9K
Despite the protective membrane that separates a cell from the environment, cells need the ability to detect and respond to environmental changes. Additionally, cells often need to communicate with one another. Unicellular and multicellular organisms use a variety of cell signaling mechanisms to communicate to respond to the environment.
129.9K
Bacterial Transformation01:33

Bacterial Transformation

59.5K
In 1928, bacteriologist Frederick Griffith worked on a vaccine for pneumonia, which is caused by Streptococcus pneumoniae bacteria. Griffith studied two pneumonia strains in mice: one pathogenic and one non-pathogenic. Only the pathogenic strain killed host mice.
Griffith made an unexpected discovery when he killed the pathogenic strain and mixed its remains with the live, non-pathogenic strain. Not only did the mixture kill host mice, but it also contained living pathogenic bacteria that...
59.5K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.6K
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...
32.6K
Endocrine Signaling01:45

Endocrine Signaling

67.9K
Endocrine cells produce hormones to communicate with remote target cells found in other organs. The hormone reaches these distant areas using the circulatory system. This exposes the whole organism to the hormone but only those cells expressing hormone receptors or target cells are affected. Thus, endocrine signaling induces slow responses from its target cells but these effects also last longer.
67.9K

You might also read

Related Articles

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

Sort by
Same author

Crystal structure of Escherichia coli type I signal peptidase P84A in complex with lipopeptide antibiotic arylomycin A<sub>2</sub>.

Journal of structural biology·2025
Same author

Functional and Structural Characterization of Treatment-Emergent Nirmatrelvir Resistance Mutations at Low Frequencies in the Main Protease (Mpro) Reveals a Unique Evolutionary Route for SARS-CoV-2 to Gain Resistance.

The Journal of infectious diseases·2025
Same author

Kinetic comparison of all eleven viral polyprotein cleavage site processing events by SARS-CoV-2 main protease using a linked protein FRET platform.

The Journal of biological chemistry·2024
Same author

A novel class of broad-spectrum active-site-directed 3C-like protease inhibitors with nanomolar antiviral activity against highly immune-evasive SARS-CoV-2 Omicron subvariants.

Emerging microbes & infections·2023
Same author

Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureus.

Nature·2023
Same author

X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation.

Nature communications·2022

Related Experiment Video

Updated: Jan 23, 2026

Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling
08:51

Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling

Published on: June 25, 2015

9.6K

Bacterial Signal Peptidases.

Mark Paetzel1

  • 1Department of Molecular Biology and Biochemistry, Simon Fraser University, South Science Building 8888 University Drive, Burnaby, BC, V5A 1S6, Canada. mpaetzel@sfu.ca.

Sub-Cellular Biochemistry
|June 20, 2019
PubMed
Summary

Signal peptidases are crucial membrane-bound enzymes. This review covers Type I (serine/lysine) and Type II (aspartic protease) bacterial signal peptidases, detailing their structure, function, and mechanisms.

Keywords:
Bacterial lipoproteinPeriplasmic proteaseProtein secretionSignal peptidaseSignal peptide

More Related Videos

The Insect Galleria mellonella as a Powerful Infection Model to Investigate Bacterial Pathogenesis
13:00

The Insect Galleria mellonella as a Powerful Infection Model to Investigate Bacterial Pathogenesis

Published on: December 11, 2012

33.3K
Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
14:05

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes

Published on: September 19, 2013

10.3K

Related Experiment Videos

Last Updated: Jan 23, 2026

Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling
08:51

Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling

Published on: June 25, 2015

9.6K
The Insect Galleria mellonella as a Powerful Infection Model to Investigate Bacterial Pathogenesis
13:00

The Insect Galleria mellonella as a Powerful Infection Model to Investigate Bacterial Pathogenesis

Published on: December 11, 2012

33.3K
Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
14:05

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes

Published on: September 19, 2013

10.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Signal peptidases are essential membrane-bound enzymes.
  • They remove signal peptides from secretory proteins during translocation.
  • Two main types exist in bacteria: Type I and Type II.

Purpose of the Study:

  • To review the known structure, function, and mechanisms of bacterial signal peptidases.
  • To highlight the distinct catalytic mechanisms of Type I and Type II enzymes.
  • To provide a comprehensive overview of these vital enzymes.

Main Methods:

  • Literature review of existing research on bacterial signal peptidases.
  • Analysis of biochemical and structural data.
  • Comparison of catalytic mechanisms and substrate specificities.

Main Results:

  • Type I signal peptidases employ a serine/lysine catalytic dyad and are widespread.
  • Type II signal peptidases function as aspartic proteases, specific for prolipoproteins.
  • Both types are integral membrane proteins with distinct active site architectures.

Conclusions:

  • Bacterial signal peptidases are diverse enzymes critical for protein secretion.
  • Understanding their structure-function relationships is key to deciphering protein processing.
  • Further research can elucidate novel roles and therapeutic targets.