scholarly journals Role of the inner-membrane histidine kinase RcsC and outer-membrane lipoprotein RcsF in the activation of the Rcs phosphorelay signal transduction system in Escherichia coli

Microbiology ◽  
2017 ◽  
Vol 163 (7) ◽  
pp. 1071-1080 ◽  
Author(s):  
Takatsugu Sato ◽  
Akira Takano ◽  
Nanako Hori ◽  
Tomoko Izawa ◽  
Takayoshi Eda ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Outer Membrane ◽  
Histidine Kinase ◽  
Signal Transduction System ◽  
Inner Membrane ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein

scholarly journals Deletion of lolB, Encoding an Outer Membrane Lipoprotein, Is Lethal for Escherichia coli and Causes Accumulation of Lipoprotein Localization Intermediates in the Periplasm

2001 ◽  
Vol 183 (22) ◽  
pp. 6538-6542 ◽  
Author(s):  
Kimie Tanaka ◽  
Shin-Ichi Matsuyama ◽  
Hajime Tokuda
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Temperature Sensitive ◽  
Helper Plasmid ◽  
Inner Membrane ◽  
Outer Membrane Lipoprotein ◽  
Lipoprotein Complex ◽  
Membrane Lipoprotein

ABSTRACT Outer membrane lipoproteins of Escherichia coli are released from the inner membrane upon the formation of a complex with a periplasmic chaperone, LolA, followed by localization to the outer membrane. In vitro biochemical analyses revealed that the localization of lipoproteins to the outer membrane generally requires an outer membrane lipoprotein, LolB, and occurs via transient formation of a LolB-lipoprotein complex. On the other hand, a mutant carrying the chromosomal lolB gene under the control of thelac promoter-operator grew normally in the absence of LolB induction if the mutant did not possess the major outer membrane lipoprotein Lpp, suggesting that LolB is only important for the localization of Lpp in vivo. To examine the in vivo function of LolB, we constructed a chromosomal lolB null mutant harboring a temperature-sensitive helper plasmid carrying the lolBgene. At a nonpermissive temperature, depletion of the LolB protein due to loss of the lolB gene caused cessation of growth and a decrease in the number of viable cells irrespective of the presence or absence of Lpp. LolB-depleted cells accumulated the LolA-lipoprotein complex in the periplasm and the mature form of lipoproteins in the inner membrane. Taken together, these results indicate that LolB is the first example of an essential lipoprotein for E. coliand that its depletion inhibits the upstream reactions of lipoprotein trafficking.

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.

scholarly journals Emerging Roles for NlpE as a Sensor for Lipoprotein Maturation and Transport to the Outer Membrane inEscherichia coli

mBio ◽  
2019 ◽  
Vol 10 (3) ◽  
Author(s):  
Brent W. Simpson ◽  
M. Stephen Trent
Keyword(s):  
Outer Membrane ◽  
Copper Stress ◽  
Gram Negative Bacteria ◽  
Two Component System ◽  
Inner Membrane ◽  
Complex Process ◽  
Outer Membrane Lipoprotein ◽  
Membrane Lipoprotein ◽  
Outer Membrane Biogenesis ◽  
Stress Pathway

ABSTRACTOuter membrane biogenesis is a complex process for Gram-negative bacteria as the components are synthesized in the cytoplasm or at the inner membrane and then transported to the outer membrane. Stress pathways monitor and respond to problems encountered in assembling the outer membrane. The two-component system CpxAR was recently reported to be a stress pathway for transport of lipoproteins to the outer membrane, but it was unclear how this stress is sensed. May et al. [K. L. May, K. M. Lehman, A. M. Mitchell, and M. Grabowicz, mBio 10(3):e00618-19, 2019,https://doi.org/10.1128/mBio.00618-19] determined that an outer membrane lipoprotein, NlpE, is the sensor for lipoprotein biogenesis stress. The group demonstrated that CpxAR is activated by the N-terminal domain of NlpE when the lipoprotein accumulates at the inner membrane. Further, this work resolved a previously debated role for NlpE in sensing copper stress; copper was shown to inhibit acylation of lipoproteins, preventing them from being transported to the outer membrane.

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