Results 31 to 40 of about 26,737 (217)

The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

open access: yesRedox Biology, 2023
The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative power and the DsbC/D system as its complement for isomerization of non-native disulfides.
Lisa R. Knoke   +6 more
doaj   +1 more source

Concerted spatio-temporal dynamics of imported DNA and ComE DNA uptake protein during gonococcal transformation.

open access: yesPLoS Pathogens, 2014
Competence for transformation is widespread among bacterial species. In the case of Gram-negative systems, a key step to transformation is the import of DNA across the outer membrane. Although multiple factors are known to affect DNA transport, little is
Heike Gangel   +6 more
doaj   +1 more source

Molecular Mechanisms of the Methionine Sulfoxide Reductase System from Neisseria meningitidis

open access: yesAntioxidants, 2018
Neisseria meningitidis, an obligate pathogenic bacterium in humans, has acquired different defense mechanisms to detect and fight the oxidative stress generated by the host’s defense during infection.
Sandrine Boschi-Muller
doaj   +1 more source

The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain

open access: yesFrontiers in Microbiology, 2021
Holin/endolysin-mediated lysis of phage T4 of Escherichia coli is tightly regulated by the antiholins RI and RIII. While regulation by the cytoplasmic RIII plays a minor role, the periplasmic antiholin RI binds tightly to the holin T and is believed to ...
Denise Mehner-Breitfeld   +4 more
doaj   +1 more source

The gram-negative bacterial periplasm: Size matters.

open access: yesPLoS Biology, 2018
Gram-negative bacteria are surrounded by two membrane bilayers separated by a space termed the periplasm. The periplasm is a multipurpose compartment separate from the cytoplasm whose distinct reducing environment allows more efficient and diverse ...
Samuel I Miller, Nina R Salama
doaj   +1 more source

DpaA Detaches Braun’s Lipoprotein from Peptidoglycan

open access: yesmBio, 2021
Gram-negative bacteria have a complex cell envelope with two membranes and a periplasm containing the peptidoglycan layer. The outer membrane is firmly connected to the peptidoglycan by highly abundant proteins.
Matthias Winkle   +8 more
doaj   +1 more source

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

open access: yesFEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka   +11 more
wiley   +1 more source

Protein O‐glycosylation in the Bacteroidota phylum

open access: yesFEBS Open Bio, EarlyView.
Species of the Bacteroidota phylum exhibit a unique O‐glycosylation system. It modifies noncytoplasmic proteins on a specific amino acid motif with a shared glycan core but a species‐specific outer glycan. A locus of multiple glycosyltransferases responsible for the synthesis of the outer glycan has been identified.
Lonneke Hoffmanns   +2 more
wiley   +1 more source

SmallTalk: a novel small‐sized fusion tag for peptide expression and purification

open access: yesFEBS Open Bio, EarlyView.
The SmallTalk fusion tag allows for the efficient expression and purification of soluble recombinant proteins or peptides in Escherichia coli. Testing with SmallTalk‐GFP confirmed that the proteins were soluble and folded correctly, while SmallTalk‐Bin1b maintained its antimicrobial activity against various bacterial isolates. This streamlined workflow
Atika Tariq   +3 more
wiley   +1 more source

Osmoregulated periplasmic glucans in Proteobacteria [PDF]

open access: yesFEMS Microbiology Letters, 2000
Large amounts of osmoregulated periplasmic glucans (OPGs) are found in the periplasmic space of Proteobacteria. Four families of OPGs are described on the basis of structural features of the polyglucose backbone. Depending on the species considered, OPGs can be modified to various extent by a variety of substituents.
openaire   +3 more sources

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