نتایج جستجو برای: periplasm

تعداد نتایج: 3548  

2017
Mauricio Cardenas‐Rodriguez Kostas Tokatlidis

Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol-reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance l...

Journal: :The Journal of Cell Biology 2007
Johannes M. Herrmann Roman Köhl

The intermembrane space (IMS) of mitochondria, the compartment that phylogenetically originated from the periplasm of bacteria, contains machinery to catalyze the oxidative folding of proteins (Mesecke, N., N. Terziyska, C. Kozany, F. Baumann, W. Neupert, K. Hell, and J.M. Herrmann. 2005. Cell. 121:1059-1069; Rissler, M., N. Wiedemann, S. Pfannschmidt, K. Gabriel, B. Guiard, N. Pfanner, and A. ...

Journal: :Journal of bacteriology 2005
Julianne H Grose Ulfar Bergthorsson Yaping Xu Jared Sterneckert Behzad Khodaverdian John R Roth

Salmonella enterica can obtain pyridine from exogenous nicotinamide mononucleotide (NMN) by three routes. In route 1, nicotinamide is removed from NMN in the periplasm and enters the cell as the free base. In route 2, described here, phosphate is removed from NMN in the periplasm by acid phosphatase (AphA), and the produced nicotinamide ribonucleoside (NmR) enters the cell via the PnuC transpor...

Journal: :Journal of embryology and experimental morphology 1980
S Takesue H Keino K Onitake

Embryogenesis in the egg of the silkworm. Bombyx mori, up to 24 h after oviposition was studied by light microscopy with special reference to nuclear migration and blastoderm formation. In Bombyx eggs blastoderm cells seem to form in a mechanism different from that usually seen in many other insect species; that is, in Bombyx eggs no typical cleavage furrows were seen. Cleavage nuclei which had...

Journal: :Philosophical transactions of the Royal Society of London. Series B, Biological sciences 2012
Badreddine Douzi Alain Filloux Romé Voulhoux

Gram-negative bacteria have evolved several secretory pathways to release enzymes or toxins into the surrounding environment or into the target cells. The type II secretion system (T2SS) is conserved in Gram-negative bacteria and involves a set of 12 to 16 different proteins. Components of the T2SS are located in both the inner and outer membranes where they assemble into a supramolecular compl...

Journal: :Journal of bacteriology 2003
Christina Wilson Bowers Fion Lau Thomas J Silhavy

LamB-LacZ fusion proteins have classically been used in studies of the general secretion pathway of Escherichia coli. Here we describe how increasing signal sequence hydrophobicity routes LamB-LacZ Hyb42-1 to the signal recognition particle (SRP) pathway. Secretion of this hydrophobic fusion variant (H*LamB-LacZ) was reduced in the absence of fully functional Ffh and Ffs, and the translocator j...

Journal: :Bioprocess and Biosystems Engineering 2006
Karolin Dresler Joop van den Heuvel Rolf-Joachim Müller Wolf-Dieter Deckwer

The hydrolase (Thermobifida fusca hydrolase; TfH) from T. fusca was produced in Escherichia coli as fusion protein using the OmpA leader sequence and a His(6) tag. Productivity could be raised more than 100-fold. Both batch and fed-batch cultivations yield comparable cell specific productivities whereas volumetric productivities differ largely. In the fed-batch cultivations final rTfH concentra...

Journal: :Journal of general microbiology 1992
K G Wooldridge J A Morrissey P H Williams

Purified [14C]aerobactin, supplied exogenously to non-growing bacteria, was translocated via the periplasm into the cytoplasm of Escherichia coli K12 strains expressing the aerobactin receptor protein IutA. No significant uptake was observed into either compartment of strains lacking the iutA gene or specifically defective in tonB. Uptake into both compartments was markedly reduced, but not abo...

2015
Kelly L Walker Alexander S Jones Colin Robinson

2015 Approximately 30% of all currently licensed, recombinantly expressed biotherapeutic products are produced in Escherichia coli, among which a significant proportion are exported to the periplasm by the general Secretory ‘Sec’ pathway. However, this pathway cannot handle many target proteins and the Tat pathway is emerging as a powerful alternative means of export. The Tat system exports ful...

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