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 Experiment Videos

A novel Escherichia coli lipoprotein expression vector

T S Jones1, V V Tryon

  • 1Department of Microbiology, University of Texas Health Science Center at San Antonio 78284-7758, USA.

Gene
|November 7, 1995
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Two-dimensional core-shell donor-acceptor assemblies at metal-organic interfaces promoted by surface-mediated charge transfer.

Nanoscale·2016
Same author

Epitaxial Templating of C60 with a Molecular Monolayer.

The journal of physical chemistry letters·2016
Same author

Determination of the individual atomic site contribution to the electronic structure of 3,4,9,10-perylene-tetracarboxylic-dianhydride (PTCDA).

The Journal of chemical physics·2013
Same author

Standard of care therapy for malignant glioma and its effect on tumor and stromal cells.

Oncogene·2011
Same author

A Case of Vesicular Mole of Unusual Size.

British medical journal·2010
Same author

Parturition in a West Indian fruit bat (Phyllostomidae).

Journal of mammalogy·2010

Researchers developed a new plasmid for Escherichia coli (Ec) to express lipoproteins. This tool enables the creation of a fusion protein for a novel signal peptidase II assay.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Escherichia coli (Ec) lipoproteins play crucial roles in bacterial cell envelope structure and function.
  • Efficient expression systems are needed to study lipoprotein processing and function.
  • Signal peptidase II (SP II) is essential for the maturation of many bacterial lipoproteins.

Purpose of the Study:

  • To construct a novel expression plasmid for Escherichia coli (Ec) to facilitate the study of lipoprotein.
  • To create a recombinant fusion protein that can be processed as a lipoprotein.
  • To develop a substrate for a novel signal peptidase II (SP II) assay.

Main Methods:

  • Construction of a novel Escherichia coli (Ec) expression plasmid, pSJLP.
  • The plasmid features a truncated alkaline phosphatase (phoA) gene fused to the signal sequence of the major Ec lipoprotein LPP.

Related Experiment Videos

  • The expression is driven by an IPTG-inducible Ptac promoter.

    • Main Results:

    • The recombinant LPP::PhoA fusion protein is successfully produced in Escherichia coli (Ec).
    • The fusion protein is processed and targeted as a lipoprotein, indicating correct signal sequence function.
    • The engineered system provides a functional substrate for signal peptidase II (SP II) activity assays.

    Conclusions:

    • The pSJLP plasmid is a valuable tool for studying Escherichia coli (Ec) lipoprotein synthesis and processing.
    • The LPP::PhoA fusion protein serves as an effective substrate for a novel signal peptidase II (SP II) assay.
    • This system advances the understanding of lipoprotein biogenesis and provides a new method for enzyme activity determination.