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BEGIN:VEVENT
DTSTAMP:20260513T082434Z
DTSTART;VALUE=DATE-TIME:20191029T120000
DTEND;VALUE=DATE-TIME:20191029T130000
SUMMARY:SLS/WMS Joint Microbiology Seminar: The outer membrane lipoprotei
 n NlpI complexes hydrolases within peptidoglycan multi-enzyme complexes 
 in Escherichia coli\, Dr Manuel Banzhaf\, School of Biosciences\, Univer
 sity of Birmingham
TZID:Europe/London
UID:20191029-8a17841a6dde8019016e16eb356b50d1@warwick.ac.uk
CREATED:20191029T094903Z
DESCRIPTION:Abstract: The peptidoglycan (PG) sacculus provides bacteria w
 ith the mechanical strength to maintain cell shape and resist osmotic st
 ress. Enlargement of the mesh-like sacculus requires the combined activi
 ty of PG synthases and hydrolases. In Escherichia coli\, the activity of
  the two bifunctional PG synthases is driven by lipoproteins anchored in
  the outer membrane. However\, the regulation of PG hydrolases is less w
 ell understood\, with only regulators for PG amidases having been descri
 bed. Here\, we identify the lipoprotein NlpI as a general adaptor protei
 n for PG hydrolases. NlpI binds to different classes of hydrolases and c
 an specifically form multimeric complexes with various PG endopeptidases
 . In addition\, NlpI seems to contribute both to PG elongation and cell 
 division biosynthetic complexes based on its localization and genetic in
 teractions. In line with such a role\, we reconstitute PG multi-enzyme c
 omplexes containing NlpI\, the PG synthesis regulator LpoA\, its cognate
  bifunctional synthase\, PBP1A\, and different endopeptidases. In additi
 on\, we find that NlpI interacts with the amidases AmiA\, Amic and the a
 midase regulator EnvC. Using an HPLC-based PG hydrolase assay we show th
 at NlpI affects the activity of AmiA in the presence or absence of EnvC.
  Our results indicate that PG regulators and adaptors are part of PG bio
 synthetic multi-enzyme complexes. Though\, our findings raise the possib
 ility that regulators are promiscuous and their regulation of PG hydrola
 ses is more complex than originally understood.
LOCATION:MBU/A151\, Medical School Building
CATEGORIES:BiomedicalSciences,DivisionalSeminars,Joint WMS/SLS Micro
LAST-MODIFIED:20191029T094903Z
ORGANIZER;CN=Jas Bains:
END:VEVENT
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