MSK
Articles
- Page Path
- HOME > J. Microbiol > Volume 59(7); 2021 > Article
-
Journal Article
- The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner
- Han Byeol Lee , Si Hyoung Park , Chang-Ro Lee
-
Journal of Microbiology 2021;59(7):666-674.
DOI: https://doi.org/10.1007/s12275-021-1130-8
Published online: May 15, 2021
-
Corresponding author:
Chang-Ro Lee , Tel: +82-31-330-6472;,
Abstract
The inner membrane protein lipopolysaccharide assembly
protein B (LapB) is an adaptor protein that activates the proteolysis
of LpxC by an essential inner membrane metalloprotease,
FtsH, leading to a decrease in the level of lipopolysaccharide
in the membrane. In this study, we revealed the
mechanism by which the essential inner membrane protein
YejM regulates LapB and analyzed the role of the transmembrane
domain of LapB in Escherichia coli. The transmembrane
domain of YejM genetically and physically interacted with
LapB and inhibited its function, which led to the accumulation
of LpxC. The transmembrane domain of LapB was indispensable
for both its physical interaction with YejM and
its regulation of LpxC proteolysis. Notably, we found that the
lapB mutant exhibited strong cold sensitivity and this phenotype
was not associated with increased accumulation of LpxC.
The transmembrane domain of LapB was also required for
its role in adaptation to cold stress. Taken together, these
results
showed that LapB plays an important role in both
the regulation of LpxC level, which is controlled by its interaction
with the transmembrane domain of YejM, and adaptation
to cold stress, which is independent of LpxC.
-
Cite this Article
- Cite this Article
-
- Close
- Download Citation
- Close
- Related articles
-
TOP
