Sequential Inactivation of Gliotoxin by the S-Methyltransferase TmtA

2016 ◽  
Vol 11 (4) ◽  
pp. 1082-1089 ◽  
Author(s):  
Elke R. Duell ◽  
Manuel Glaser ◽  
Camille Le Chapelain ◽  
Iris Antes ◽  
Michael Groll ◽  
...  
Keyword(s):  
Sequential Inactivation

Sequential inactivation of ζ-crystallin by o-phthalaldehyde

2002 ◽  
Vol 1597 (1) ◽  
pp. 67-73
Author(s):  
Mohammad D. Bazzi ◽  
Nayyar Rabbani ◽  
Ali S. Duhaiman
Keyword(s):  
Sequential Inactivation

scholarly journals FadD19 of Rhodococcus rhodochrous DSM43269, a Steroid-Coenzyme A Ligase Essential for Degradation of C-24 Branched Sterol Side Chains

2011 ◽  
Vol 77 (13) ◽  
pp. 4455-4464 ◽  
Author(s):  
M. H. Wilbrink ◽  
M. Petrusma ◽  
L. Dijkhuizen ◽  
R. van der Geize
Keyword(s):  
Mutant Strain ◽  
Coenzyme A ◽  
Side Chain ◽  
Side Chains ◽  
Rhodococcus Rhodochrous ◽  
Content Type ◽  
Coa Ligase ◽  
Coenzyme A Ligase ◽  
Sequential Inactivation

ABSTRACTThe actinobacterial cholesterol catabolic gene cluster contains a subset of genes that encode β-oxidation enzymes with a putative role in sterol side chain degradation. We investigated the physiological roles of several genes, i.e.,fadD17,fadD19,fadE26,fadE27, andro04690DSM43269, by gene inactivation studies in mutant strain RG32 ofRhodococcus rhodochrousDSM43269. Mutant strain RG32 is devoid of 3-ketosteroid 9α-hydroxylase (KSH) activity and was constructed following the identification, cloning, and sequential inactivation of fivekshAgene homologs in strain DSM43269. We show that mutant strain RG32 is fully blocked in steroid ring degradation but capable of selective sterol side chain degradation. Except for RG32ΔfadD19, none of the mutants constructed in RG32 revealed an aberrant phenotype on sterol side chain degradation compared to parent strain RG32. Deletion offadD19in strain RG32 completely blocked side chain degradation of C-24 branched sterols but interestingly not that of cholesterol. The additional inactivation offadD17in mutant RG32ΔfadD19also did not affect cholesterol side chain degradation. Heterologously expressed FadD19DSM43269nevertheless was active toward steroid-C26-oic acid substrates. Our data identified FadD19 as a steroid-coenzyme A (CoA) ligase with an essentialin vivorole in the degradation of the side chains of C-24 branched-chain sterols. This paper reports the identification and characterization of a CoA ligase with anin vivorole in sterol side chain degradation. The high similarity (67%) between the FadD19DSM43269and FadD19H37Rvenzymes further suggests that FadD19H37Rvhas anin vivorole in sterol metabolism ofMycobacterium tuberculosisH37Rv.

scholarly journals Deactivation of Ascaris suum eggs using electroporation and sequential inactivation with chemical disinfection

2020 ◽  
Vol 10 (3) ◽  
pp. 558-568
Author(s):  
C. Niven ◽  
C. B. Parker ◽  
S. D. Wolter ◽  
M. H. Dryzer ◽  
C. B. Arena ◽  
...  
Keyword(s):  
Pulse Train ◽  
Ascaris Suum ◽  
Chemical Exposure ◽  
Alternative Technique ◽  
Buffer Solution ◽  
Helminth Eggs ◽  
Low Concentrations ◽  
Pass Through ◽  
Sequential Inactivation ◽  
Initial Results

Abstract Electroporation has been evaluated as a potential backend wastewater treatment for deactivation of Ascaris suum eggs in buffer solution. Initial results indicate that eggshell permeability is affected by the pulse train electric field strength and duration. Coupling electroporation with chemical exposure, using low concentrations of commercially available disinfectants, allows oxidizing agents to pass through the complex strata of the A. suum eggshell, specifically reaching the innermost embryonic environment, which leads to successful deactivation compared to either method used separately. The aim of this work is to identify and develop an alternative technique that efficiently inactivates helminth eggs present in wastewater.

scholarly journals Golgi Inheritance in Mammalian Cells Is Mediated through Endoplasmic Reticulum Export Activities

2006 ◽  
Vol 17 (2) ◽  
pp. 990-1005 ◽  
Author(s):  
Nihal Altan-Bonnet ◽  
Rachid Sougrat ◽  
Wei Liu ◽  
Erik L. Snapp ◽  
Theresa Ward ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mammalian Cells ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Transmembrane Proteins ◽  
Temperature Sensitive ◽  
Golgi Membranes ◽  
Sequential Inactivation ◽  
Er Export ◽  
Microscopy Techniques

Golgi inheritance during mammalian cell division occurs through the disassembly, partitioning, and reassembly of Golgi membranes. The mechanisms responsible for these processes are poorly understood. To address these mechanisms, we have examined the identity and dynamics of Golgi proteins within mitotic membranes using live cell imaging and electron microscopy techniques. Mitotic Golgi fragments, seen in prometaphase and telophase, were found to localize adjacent to endoplasmic reticulum (ER) export domains, and resident Golgi transmembrane proteins cycled rapidly into and out of these fragments. Golgi proteins within mitotic Golgi haze—seen during metaphase—were found to redistribute with ER markers into fragments when the ER was fragmented by ionomycin treatment. The temperature-sensitive misfolding mutant ts045VSVG protein, when localized to the Golgi at the start of mitosis, became trapped in the ER at the end of mitosis in cells shifted to 40°C. Finally, reporters for Arf1 and Sar1 activity revealed that Arf1 and Sar1 undergo sequential inactivation during mitotic Golgi breakdown and sequential reactivation upon Golgi reassembly at the end of mitosis. Together, these findings support a model of mitotic Golgi inheritance that involves inhibition and subsequent reactivation of cellular activities controlling the cycling of Golgi components into and out of the ER.

scholarly journals Benefit of Having Multiple ampD Genes for Acquiring β-Lactam Resistance without Losing Fitness and Virulence in Pseudomonas aeruginosa

2008 ◽  
Vol 52 (10) ◽  
pp. 3694-3700 ◽  
Author(s):  
Bartolomé Moya ◽  
Carlos Juan ◽  
Sebastián Albertí ◽  
José L. Pérez ◽  
Antonio Oliver
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Mouse Model ◽  
Resistance Mechanism ◽  
Systemic Infection ◽  
Triple Mutant ◽  
Biological Cost ◽  
Sequential Inactivation ◽  
High Level ◽  
Insight Into

ABSTRACT The inactivation of ampD in Pseudomonas aeruginosa leads to a partially derepressed phenotype, characterized by a moderately high level basal ampC expression that is still further inducible, due to the presence of two additional ampD genes in this species (ampDh2 and ampDh3). The sequential inactivation of the three ampD genes was shown to lead to a stepwise upregulation of ampC expression, reaching full derepression in the triple mutant. To gain insight into the biological role of P. aeruginosa AmpD multiplicity, we determined the effects of the inactivation of the ampD genes on fitness and virulence. We show that, in contrast to what was previously documented for Salmonella spp., the inactivation of ampD in P. aeruginosa does not affect fitness or virulence in a mouse model of systemic infection. This lack of effect was demonstrated to be dependent on the presence of the additional ampD genes (ampDh2 and ampDh3), since the double and the triple ampD mutants completely lost their biological competitiveness and virulence; full ampC derepression and disruption of the AmpD peptidoglycan recycling system itself are both found to cause a major biological cost. Furthermore, among the ampD genes, ampDh3 is found to be the most relevant for virulence in P. aeruginosa. Therefore, as a consequence of the presence of additional ampD genes, partial ampC derepression mediated by ampD inactivation confers a biologically efficient resistance mechanism on P. aeruginosa.

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