onr:"swepub:oai:DiVA.org:umu-212079"
Search: onr:"swepub:oai:DiVA.org:umu-212079" > EstG is a novel est...
- 1 of 1
- Previous record
- Next record
- To hitlist
EstG is a novel esterase required for cell envelope integrity in Caulobacter
-
- Daitch, Allison K. (author)
- Department of Biological Chemistry, Johns Hopkins University School of Medicine, MD, Baltimore, United States
-
- Orsburn, Benjamin C. (author)
- Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, MD, Baltimore, United States
-
- Chen, Zan (author)
- Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, MD, Baltimore, United States
- show more...
- show less...
- (creator_code:org_t)
- Cell Press, 2023
- 2023
- English.
- In: Current Biology. - : Cell Press. - 0960-9822 .- 1879-0445. ; 33:2, s. 228-240.e7
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- Proper regulation of the bacterial cell envelope is critical for cell survival. Identification and characterization of enzymes that maintain cell envelope homeostasis is crucial, as they can be targets for effective antibiotics. In this study, we have identified a novel enzyme, called EstG, whose activity protects cells from a variety of lethal assaults in the ⍺-proteobacterium Caulobacter crescentus. Despite homology to transpeptidase family cell wall enzymes and an ability to protect against cell-wall-targeting antibiotics, EstG does not demonstrate biochemical activity toward cell wall substrates. Instead, EstG is genetically connected to the periplasmic enzymes OpgH and BglX, responsible for synthesis and hydrolysis of osmoregulated periplasmic glucans (OPGs), respectively. The crystal structure of EstG revealed similarities to esterases and transesterases, and we demonstrated esterase activity of EstG in vitro. Using biochemical fractionation, we identified a cyclic hexamer of glucose as a likely substrate of EstG. This molecule is the first OPG described in Caulobacter and establishes a novel class of OPGs, the regulation and modification of which are important for stress survival and adaptation to fluctuating environments. Our data indicate that EstG, BglX, and OpgH comprise a previously unknown OPG pathway in Caulobacter. Ultimately, we propose that EstG is a novel enzyme that instead of acting on the cell wall, acts on cyclic OPGs to provide resistance to a variety of cellular stresses.
Subject headings
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Keyword
- antibiotics
- Caulobacter crescentus
- cell envelope
- envelope stress
- esterase
- Gram-negative
- osmoregulated periplasmic glucans
- peptidoglycan
- transesterase
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- Current Biology (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Daitch, Allison ...
- Orsburn, Benjami ...
- Chen, Zan
- Alvarez, Laura
- Eberhard, Colten ...
- Sundararajan, Ko ...
- show more...
- Zeinert, Rilee
- Kreitler, Dale F ...
- Jakoncic, Jean
- Chien, Peter
- Cava, Felipe
- Gabelli, Sandra ...
- Goley, Erin D.
- show less...
- About the subject
-
- NATURAL SCIENCES
- NATURAL SCIENCES
- and Biological Scien ...
- and Microbiology
- Articles in the publication
- Current Biology
- By the university
- Umeå University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
