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Production of Recombinant Rhomboid Proteases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00483405" target="_blank" >RIV/61388963:_____/17:00483405 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/bs.mie.2016.10.031" target="_blank" >http://dx.doi.org/10.1016/bs.mie.2016.10.031</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/bs.mie.2016.10.031" target="_blank" >10.1016/bs.mie.2016.10.031</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Production of Recombinant Rhomboid Proteases

  • Original language description

    Rhomboid proteases are intramembrane enzymes that hydrolyze peptide bonds of transmembrane proteins in the lipid bilayer. They play a variety of roles in key biological events and are linked to several disease states. Over the last decade a great deal of structural and functional knowledge has been generated on this fascinating class of proteases. Both structural and kinetic analyses require milligram amounts of protein, which may be challenging for membrane proteins such as rhomboids. Here, we present a detailed protocol for optimization of expression and purification of three rhomboid proteases from Escherichia coli (ecGlpG), Haemophilus influenzae (hiGlpG), and Providencia stuartii (AarA). We discuss the optimization of expression conditions, such as concentration of inducing agent, induction time, and temperature, as well as purification protocol with precise details for each step. The provided protocol yields 1-2.5 mg of rhomboid enzyme per liter of bacterial culture and can assist in structural and functional studies of intramembrane proteases.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Book/collection name

    Enzymology at the Membrane Interface: Intramembrane Proteases

  • ISBN

    978-0-12-812213-6

  • Number of pages of the result

    24

  • Pages from-to

    255-278

  • Number of pages of the book

    474

  • Publisher name

    Academic Press

  • Place of publication

    Cambridge

  • UT code for WoS chapter

    000403271000011