Cover Picture: Catch‐and‐Release Probes Applied to Semi‐Intact Cells Reveal Ubiquitin‐Specific Protease Expression in Chlamydia trachomatis Infection (ChemBioChem 3/2013). Issue 3 (6th February 2013)
- Record Type:
- Journal Article
- Title:
- Cover Picture: Catch‐and‐Release Probes Applied to Semi‐Intact Cells Reveal Ubiquitin‐Specific Protease Expression in Chlamydia trachomatis Infection (ChemBioChem 3/2013). Issue 3 (6th February 2013)
- Main Title:
- Cover Picture: Catch‐and‐Release Probes Applied to Semi‐Intact Cells Reveal Ubiquitin‐Specific Protease Expression in Chlamydia trachomatis Infection (ChemBioChem 3/2013)
- Authors:
- Claessen, Jasper H. L.
Witte, Martin D.
Yoder, Nicholas C.
Zhu, Angela Y.
Spooner, Eric
Ploegh, Hidde L. - Abstract:
- <abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The cover picture shows the delivery of a novel catch‐and‐release ubiquitin probe to cells infected with <italic>Chlamydia trachomatis.</italic> Protein ubiquitylation serves as a versatile signal involved in all areas of cell biology, and is controlled by a class of de‐ubiquitylating enzymes (DUBs). In the article on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 343 ff, H. L.</ext-link> Ploegh et al. report an activity‐based probe that covalently binds to DUBs. Sortase‐mediated chemistry allowed three different cleavable linker handles to be installed on the probe, and this resulted in the efficient retrieval of bound protein. As the probe is cell impermeable, it was delivered to the cytosol of cells permeabilized with the pore‐forming toxin perfringolysin O. With this technique, the authors were able to identify great numbers of DUBs at endogenous expression level. When the technique was applied to cells infected with <italic>C. trachomatis</italic>, the authors observed expression of different host DUBs and identified two DUBs expressed by the pathogen itself. The cover was designed by Tom DiCesare (Whitehead Institute for Biomedical Research).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1tsjwjp0"<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The cover picture shows the delivery of a novel catch‐and‐release ubiquitin probe to cells infected with <italic>Chlamydia trachomatis.</italic> Protein ubiquitylation serves as a versatile signal involved in all areas of cell biology, and is controlled by a class of de‐ubiquitylating enzymes (DUBs). In the article on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">p. 343 ff, H. L.</ext-link> Ploegh et al. report an activity‐based probe that covalently binds to DUBs. Sortase‐mediated chemistry allowed three different cleavable linker handles to be installed on the probe, and this resulted in the efficient retrieval of bound protein. As the probe is cell impermeable, it was delivered to the cytosol of cells permeabilized with the pore‐forming toxin perfringolysin O. With this technique, the authors were able to identify great numbers of DUBs at endogenous expression level. When the technique was applied to cells infected with <italic>C. trachomatis</italic>, the authors observed expression of different host DUBs and identified two DUBs expressed by the pathogen itself. The cover was designed by Tom DiCesare (Whitehead Institute for Biomedical Research).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1tsjwjp0" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract> … (more)
- Is Part Of:
- Chembiochem. Volume 14:Issue 3(2013)
- Journal:
- Chembiochem
- Issue:
- Volume 14:Issue 3(2013)
- Issue Display:
- Volume 14, Issue 3 (2013)
- Year:
- 2013
- Volume:
- 14
- Issue:
- 3
- Issue Sort Value:
- 2013-0014-0003-0000
- Page Start:
- 269
- Page End:
- 269
- Publication Date:
- 2013-02-06
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pharmaceutical chemistry -- Periodicals
572 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7633 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cbic.201390004 ↗
- Languages:
- English
- ISSNs:
- 1439-4227
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3133.490980
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3679.xml