ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Publication Date: 2011-07-22
    Description: Peptidoglycan is the major structural constituent of the bacterial cell wall, forming a meshwork outside the cytoplasmic membrane that maintains cell shape and prevents lysis. In Gram-negative bacteria, peptidoglycan is located in the periplasm, where it is protected from exogenous lytic enzymes by the outer membrane. Here we show that the type VI secretion system of Pseudomonas aeruginosa breaches this barrier to deliver two effector proteins, Tse1 and Tse3, to the periplasm of recipient cells. In this compartment, the effectors hydrolyse peptidoglycan, thereby providing a fitness advantage for P. aeruginosa cells in competition with other bacteria. To protect itself from lysis by Tse1 and Tse3, P. aeruginosa uses specific periplasmically localized immunity proteins. The requirement for these immunity proteins depends on intercellular self-intoxication through an active type VI secretion system, indicating a mechanism for export whereby effectors do not access donor cell periplasm in transit.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3146020/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3146020/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, Alistair B -- Hood, Rachel D -- Bui, Nhat Khai -- LeRoux, Michele -- Vollmer, Waldemar -- Mougous, Joseph D -- R01 AI080609/AI/NIAID NIH HHS/ -- R01 AI080609-03/AI/NIAID NIH HHS/ -- England -- Nature. 2011 Jul 20;475(7356):343-7. doi: 10.1038/nature10244.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Washington, Seattle, Washington 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21776080" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/chemistry/genetics/metabolism ; Amino Acid Sequence ; Bacterial Proteins/antagonists & ; inhibitors/chemistry/genetics/*metabolism/secretion ; *Bacterial Secretion Systems ; Bacterial Toxins/antagonists & inhibitors/metabolism ; *Bacteriolysis ; Gram-Negative Bacteria/*cytology/*metabolism ; Hydrolysis ; *Microbial Interactions ; Muramidase/chemistry/genetics/metabolism ; Peptidoglycan/metabolism ; Periplasm/metabolism ; Pseudomonas aeruginosa/enzymology/genetics/growth & development/*metabolism ; Pseudomonas putida/growth & development/metabolism ; Substrate Specificity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...