scholarly journals Aerobic Activity of Escherichia coliAlcohol Dehydrogenase Is Determined by a Single Amino Acid

2000 ◽  
Vol 182 (21) ◽  
pp. 6049-6054 ◽  
Author(s):  
Carol A. Holland-Staley ◽  
KangSeok Lee ◽  
David P. Clark ◽  
Philip R. Cunningham
Keyword(s):  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Structural Gene ◽  
Genetic Selection ◽  
Site Directed Mutagenesis ◽  
Single Amino Acid ◽  
Expression Vectors ◽  
Anaerobic Conditions ◽  
Aerobic And Anaerobic ◽  
Aerobic And Anaerobic Conditions

ABSTRACT Expression of the alcohol dehydrogenase gene, adhE, inEscherichia coli is anaerobically regulated at both the transcriptional and the translational levels. To study the AdhE protein, the adhE + structural gene was cloned into expression vectors under the control of the lacZ andtrp c promoters. Wild-type AdhE protein produced under aerobic conditions from these constructs was inactive. Constitutive mutants (adhC) that produced high levels of AdhE under both aerobic and anaerobic conditions were previously isolated. When only the adhE structural gene from one of the adhC mutants was cloned into expression vectors, highly functional AdhE protein was isolated under both aerobic and anaerobic conditions. Sequence analysis revealed that the adhE gene from the adhC mutant contained two mutations resulting in two amino acid substitutions, Ala267Thr and Glu568Lys. Thus,adhC strains contain a promoter mutation and two mutations in the structural gene. The mutant structural gene fromadhC strains was designated adhE*. Fragment exchange experiments revealed that the substitution responsible for aerobic expression in the adhE* clones is Glu568Lys. Genetic selection and site-directed mutagenesis experiments showed that virtually any amino acid substitution for Glu568 produced AdhE that was active under both aerobic and anaerobic conditions. These findings suggest that adhE expression is also regulated posttranslationally and that strict regulation of alcohol dehydrogenase activity in E. coli is physiologically significant.

scholarly journals Single amino acid changes in the mumps virus haemagglutinin–neuraminidase and polymerase proteins are associated with neuroattenuation

2009 ◽  
Vol 90 (7) ◽  
pp. 1741-1747 ◽  
Author(s):  
Tahir H. Malik ◽  
Candie Wolbert ◽  
Laura Nerret ◽  
Christian Sauder ◽  
Steven Rubin
Keyword(s):  
Amino Acid ◽  
Clinical Isolate ◽  
Amino Acid Change ◽  
Mumps Virus ◽  
Site Directed Mutagenesis ◽  
Single Amino Acid ◽  
Supporting Evidence ◽  
L Protein ◽  
Single Amino Acid Change

It has previously been shown that three amino acid changes, one each in the fusion (F; Ala/Thr-91→Thr), haemagglutinin–neuraminidase (HN; Ser-466→Asn) and polymerase (L; Ile-736→Val) proteins, are associated with attenuation of a neurovirulent clinical isolate of mumps virus (88-1961) following serial passage in vitro. Here, using full-length cDNA plasmid clones and site-directed mutagenesis, it was shown that the single amino acid change in the HN protein and to a lesser extent, the change in the L protein, resulted in neuroattenuation, as assessed in rats. The combination of both amino acid changes caused neuroattenuation of the virus to levels previously reported for the clinical isolate following attenuation in vitro. The amino acid change in the F protein, despite having a dramatic effect on protein function in vitro, was previously shown to not be involved in the observed neuroattenuation, highlighting the importance of conducting confirmatory in vivo studies. This report provides additional supporting evidence for the role of the HN protein as a virulence factor and, as far as is known, is the first report to associate an amino acid change in the L protein with mumps virus neuroattenuation.

Oxygen concentration affects frequency and range of transconjugants for the incompatibility (Inc) P-1 and P-7 plasmids pBP136 and pCAR1

2020 ◽  
Vol 85 (4) ◽  
pp. 1005-1015
Author(s):  
Kentaro Ochi ◽  
Maho Tokuda ◽  
Kosuke Yanagiya ◽  
Chiho Suzuki-Minakuchi ◽  
Hideaki Nojiri ◽  
...  
Keyword(s):  
Oxygen Concentration ◽  
Anaerobic Condition ◽  
Environmental Samples ◽  
Aerobic Condition ◽  
Recipient Strain ◽  
Donor Strain ◽  
Anaerobic Conditions ◽  
Filter Mating ◽  
Aerobic And Anaerobic ◽  
Aerobic And Anaerobic Conditions

ABSTRACT The frequency of transconjugants were compared for the incompatibility (Inc) P-1 and P-7 plasmids pBP136 and pCAR1 under aerobic and anaerobic conditions. Filter mating assays were performed with one donor strain and one recipient strain using different donors of Pseudomonas and recipient strains, including Pseudomonas, Pantoea, and Buttiauxella. Under anaerobic condition, frequencies of transconjugants for both plasmids were 101-103-fold lower than those under aerobic condition regardless of whether aerobically or anaerobically grown donors and recipients were used. To compare the transconjugant ranges under aerobic and anaerobic conditions, conjugation was performed between the donor of pBP136 and recipient bacteria extracted from environmental samples. Several transconjugants were uniquely obtained from each aerobic or anaerobic condition. Our findings indicate that a plasmid can differently spread among bacteria depending on the oxygen concentrations of the environment.

PRODUCTION AND PROPERTIES OF 2,3-BUTANEDIOL: VII. FERMENTATION OF WHEAT BY AEROBACILLUS POLYMYXA UNDER AEROBIC AND ANAEROBIC CONDITIONS

1946 ◽  
Vol 24f (1) ◽  
pp. 1-11 ◽  
Author(s):  
G. A. Adams
Keyword(s):  
Carbon Dioxide ◽  
Anaerobic Fermentation ◽  
Anaerobic Conditions ◽  
Mechanical Agitation ◽  
Fermentation Time ◽  
Aerobic Conditions ◽  
Ethanol Formation ◽  
Time Required ◽  
Aerobic And Anaerobic ◽  
Aerobic And Anaerobic Conditions

Aeration by mechanical agitation of 15% wheat mash fermented by Aerobacillus polymyxa inhibited the formation of 2,3-butanediol and particularly of ethanol. Aeration of similar mashes by passage of finely dispersed air or oxygen at the rate of 333 ml. per minute per litre of mash increased the rate of formation and yield of 2,3-butanediol but inhibited ethanol formation. However, the over-all time required for the completion of fermentation was not shortened from the usual 72 to 96 hr. required for unaerated mashes. There was no evidence of a shift from fermentative to oxidative dissimilation. Under aerobic conditions, the final butanediol–ethanol ratio was approximately 3:1. Anaerobic conditions, as produced by the passage of nitrogen or hydrogen through the mash, increased the rate of formation of both butanediol and ethanol and shortened the fermentation time to about 48 hr. Under these conditions, the butanediol–ethanol ratio was reduced to about 1.3:1.0. Carbon dioxide gave a butanediol–ethanol ratio resembling that of anaerobic fermentation but did not reduce fermentation time.

scholarly journals Optimizing characteristics in mineral insulating oil used in high power transformers

2019 ◽  
pp. 222-228
Author(s):  
Irina Alina Chera Anghel ◽  
Loredana Popescu
Keyword(s):  
Mineral Oil ◽  
The Other ◽  
Power Transformers ◽  
Anaerobic Conditions ◽  
Mineral Oils ◽  
Insulating Liquid ◽  
Different Characteristics ◽  
Aerobic And Anaerobic ◽  
Good Heat ◽  
Aerobic And Anaerobic Conditions

The most commonly used insulating liquid in transformers is mineral oil. Special synthetic applications such as silicone, ester, perchloroethene, etc. are used today in special applications, with different characteristics, very low or nonexistent toxicity to mineral oils used in transformers. On the other hand, they have a much better biodegradability than mineral oils in both aerobic and anaerobic conditions. But they cannot directly replace the mineral oil in operation or in repaired units. They have dielectric properties and good heat transfer but have limited their use to special transformers due to the relatively high cost and availability.

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