scholarly journals Membrane Stress Caused by Unprocessed Outer Membrane Lipoprotein Intermediate Pro-Lpp Affects DnaA and Fis-Dependent Growth

2021 ◽  
Vol 12 ◽  
Author(s):  
Digvijay Patil ◽  
Dan Xun ◽  
Markus Schueritz ◽  
Shivani Bansal ◽  
Amrita Cheema ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Physiological State ◽  
Cell Mass ◽  
Ectopic Expression ◽  
Close Link ◽  
Small Regulatory Rna ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein ◽  
Dependent Growth ◽  
In Cells

In Escherichia coli, repression of phosphatidylglycerol synthase A gene (pgsA) lowers the levels of membrane acidic phospholipids, particularly phosphatidylglycerol (PG), causing growth-arrested phenotype. The interrupted synthesis of PG is known to be associated with concomitant reduction of chromosomal content and cell mass, in addition to accumulation of unprocessed outer membrane lipoprotein intermediate, pro-Lpp, at the inner membrane. However, whether a linkage exists between the two altered-membrane outcomes remains unknown. Previously, it has been shown that pgsA+ cells overexpressing mutant Lpp(C21G) protein have growth defects similar to those caused by the unprocessed pro-Lpp intermediate in cells lacking PG. Here, we found that the ectopic expression of DnaA(L366K) or deletion of fis (encoding Factor for Inversion Stimulation) permits growth of cells that otherwise would be arrested for growth due to accumulated Lpp(C21G). The DnaA(L366K)-mediated restoration of growth occurs by reduced expression of Lpp(C21G) via a σE-dependent small-regulatory RNA (sRNA), MicL-S. In contrast, restoration of growth via fis deletion is only partially dependent on the MicL-S pathway; deletion of fis also rescues Lpp(C21G) growth arrest in cells lacking physiological levels of PG and cardiolipin (CL), independently of MicL-S. Our results suggest a close link between the physiological state of the bacterial cell membrane and DnaA- and Fis-dependent growth.

Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis

2012 ◽  
Vol 8 (1) ◽  
pp. 53-55 ◽  
Author(s):  
Ladislav Bumba ◽  
Ekaterina Sviridova ◽  
Ivana Kutá Smatanová ◽  
Pavlína Řezáčová ◽  
Václav Veverka
Keyword(s):  
Neisseria Meningitidis ◽  
Outer Membrane ◽  
Resonance Assignments ◽  
Backbone Resonance Assignments ◽  
Backbone Resonance ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein

scholarly journals Role of the Pilot Protein YscW in the Biogenesis of the YscC Secretin in Yersinia enterocolitica

2004 ◽  
Vol 186 (16) ◽  
pp. 5366-5375 ◽  
Author(s):  
Peter Burghout ◽  
Frank Beckers ◽  
Emmie de Wit ◽  
Ria van Boxtel ◽  
Guy R. Cornelis ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Yersinia Enterocolitica ◽  
Amino Acid Residues ◽  
Wild Type ◽  
C Terminus ◽  
Outer Membrane Lipoprotein ◽  
Protein Secretion System ◽  
Membrane Lipoprotein ◽  
Type Iii Protein Secretion

ABSTRACT The YscC secretin is a major component of the type III protein secretion system of Yersinia enterocolitica and forms an oligomeric structure in the outer membrane. In a mutant lacking the outer membrane lipoprotein YscW, secretion is strongly reduced, and it has been proposed that YscW plays a role in the biogenesis of the secretin. To study the interaction between the secretin and this putative pilot protein, YscC and YscW were produced in trans in a Y. enterocolitica strain lacking all other components of the secretion machinery. YscW expression increased the yield of oligomeric YscC and was required for its outer membrane localization, confirming the function of YscW as a pilot protein. Whereas the pilot-binding site of other members of the secretin family has been identified in the C terminus, a truncated YscC derivative lacking the C-terminal 96 amino acid residues was functional and stabilized by YscW. Pulse-chase experiments revealed that ∼30 min were required before YscC oligomerization was completed. In the absence of YscW, oligomerization was delayed and the yield of YscC oligomers was strongly reduced. An unlipidated form of the YscW protein was not functional, although it still interacted with the secretin and caused mislocalization of YscC even in the presence of wild-type YscW. Hence, YscW interacts with the unassembled YscC protein and facilitates efficient oligomerization, likely at the outer membrane.

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