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S Benson

Publications and source records attributed to S Benson.

At least 73 records · Page 4Linked to original sources
PubMed1982

Genetic approaches to study export of LamB to the outer membrane.

We are studying the molecular mechanism of cellular protein localization. The availability of genetic techniques, such as gene fusion in Escherichia coli, has made this subject particularly amenable to study in this prokaryote. We have constructed a variety of strains in which the gene coding for an outer membrane protein is fused to the gene coding for a normally cytoplasmic enzyme, beta-galactosidase. The hybrid protein produced by such strains retain beta-galactosidase activity; this activity serves as a simple biochemical tag for studying the localization of the outer membrane protein. In addition, we have exploited phenotypes exhibited by certain fusion strains to isolate mutants that are altered in the process of protein export. Genetic and biochemical analyses of such mutants have provided important insights into the mechanism of protein localization.

Amino Acid Sequence↗
PubMed1981

The effect of intravenous therapy during labour on maternal and cord serum sodium levels.

A total of 113 women in labour were studied prospectively to determine the relation between maternal and cord serum sodium levels and the effect of intravenous infusions of glucose solutions and oxytocin during labour on the mother and infant. Maternal and cord sodium levels were correlated, with no systematic difference between the two, which is consistent with passive diffusion of sodium across the placenta. Glucose infusions and oxytocin caused statistically significant depression of maternal and cord serum sodium levels, but with the quantities used this did not adversely affect the mothers or infants. It is recommended that caution should be exercised in prescribing intravenous therapy during labour and, if more than 500 ml of fluid is required, sodium should be included.

Female↗
PubMed1979

Insertion element analysis and mapping of the Pseudomonas plasmid alk regulon.

We characterized and mapped new mutations of the alk (alkane utilization) genes found on Pseudomonas plasmids of the Inc P-2 group. These mutations were isolated after (i) nitrosoguanidine mutagenesis, (ii) transposition of the Tn7 trimethoprim and streptomycin resistance determinant, and (iii) reversion of polarity effects of alk::Tn7 insertion mutations. Our results indicate the existence of two alk loci not previously described--alkD, whose product is required for synthesis of membrane alkane-oxidizing activities, and alkE, whose product is required for synthesis of inducible membrane alcohol dehydrogenase activity. Polarity of alk::Tn7 insertion mutations indicates the existence of an alkBAE operon. Mapping of alk loci by transduction in P. aeruginosa shows that there are at least three alk clusters in the CAM-OCT plasmid--alkRD, containing regulatory genes; alkBAE, containing genes for specific biochemical activities; and alkC, containing one or more genes needed for normal synthesis of membrane alcohol dehydrogenase. The alkRD and alkBAE clusters are linked but separated by about 42 kilobases. The alkC cluster is not linked to either of the other two alk regions. Altogether, these results indicate a complex genetic control of the alkane utilization phenotype in P. putida and P. aeruginosa involving at least six separate genes.

Alkanes↗
PubMed1979

Regulation of membrane peptides by the Pseudomonas plasmid alk regulon.

Pseudomonas putida strains carrying the plasmid alk genes will grow on n-alkanes. Induced alk+ strains contain membrane activities for alkane hydroxylation and dehydrogenation of aliphatic primary alcohols. P. putida cytoplasmic and outer membranes can be separated by sucrose gradient centrifugation after disruption of cells by either mild detergent lysis or passage through a French press. Both the membrane component of alkane hydroxylase and membrane alcohol dehydrogenase fractionated with the cytoplasmic membrane. Induction of the alk regulon resulted in the appearance of at least three new plasmid-determined cytoplasmic membrane peptides of about 59,000 (59K), 47,000 (47K), and 40,000 (40K) daltons as well as the disappearance of a pair of chromosomally encoded outer membrane peptides of about 43,000 daltons. The 40K peptide is the membrane component of alkane hydroxylase and the product of the plasmid alkB gene because the alkB1029 mutation altered the properties of alkane hydroxylase in whole cells, reduced its thermal stability in cell extracts, and led to increased electrophoretic mobility of the inducible 40K peptide. These results are consistent with a model for vectorial oxidation of n-alkanes in the cytoplasmic membrane of P. putida.

Alkanes↗
PubMed1978

TOL is a broad-host-range plasmid.

We readily isolated insertions of the carbenicillin resistance element Tn401 into the TOL plasmid in Pseudomonas putida. Hybrid TOL::Tn401 plasmids stably express the Cbr phenotype in Pseudomonas aeruginosa and Escherichia coli. Whereas the replicative and conjugative functions are expressed in both hosts, the ability to grow on m-toluate is only expressed in the Pseudomonas species.

Conjugation, Genetic↗
PubMed1977

Fractionation of inducible alkane hydroxylase activity in Pseudomonas putida and characterization of hydroxylase-negative plasmid mutations.

The plasmid-determined inducible alkane hydroxylase of Pseudomonas putida resolved into particulate and soluble fractions. Spinach reductase and spinach ferredoxin could replace the soluble hydroxylase component. Two alkane hydroxylase mutants show in vitro complementation (S. Benson and J. Shapiro, J. Bacteriol., 123: 759-760, 1975): one, alk-7, lacks an active soluble component and the other, alk-181, lacks an active particulate component. Together with previous results on a particulate alcohol dehydrogenase enzyme (Benson and Shapiro, J. Bacteriol., 126: 794-798, 1976), these results allowed us to assay three plasmid-determined inducible activities: soluble alkane hydroxylase (alkA+), particulate alkane hydroxylase (alkB+), and particulate alcohol dehydrogenase (alkC+). Growth tests and in vitro complementation assays revealed three groups of plasmid mutations that block expression of alkane hydroxylase activity: alkA, which so far includes only the alk-7 mutation; alkB, which includes alk-181 and 11 other mutations; and a pleiotropic-negative class, which includes nine mutations that lead to loss of alkA+, alkB+, and alkC+ activities. Thus, the alk+ gene cluster found on IncP-2 plasmids contains at least four cistrons. We believe it is significant that two of these determined the presence of membrane proteins. The accompanying paper shows that these loci are part of a single regulon.

Alkanes↗
PubMed1976

Protective effect of elongation factor 2 on the inactivation of ribosomes by the toxic lectins abrin and ricin.

The inactivation of rabbit reticulocyte ribosomes by abrin and ricin A-chains was studied by incubating ribosomes with the A-chains and testing, after various periods of time, aliquots of the ribosomes for their ability to polymerize phenylalanine. The presence of elongation factor 2 (EF-2) reduced the rate of inactivation of ribosomes by the A-chains. The protective effect of EF-2 was strongly enhanced by GTP and, to a lesser extent, also by GDP or dGTP. Other nucleotides had no demonstrable effect. Much less protection was found after binding of Phe-tRNA to ribosomes in the presence of EF-1 (enzymic binding) or in the presence of high Mg2+ concentration (non-enzymic binding). The data indicate that when EF-2 binds to the ribosomes it completely or partially covers the target site for abrin and ricin A-chains. The possibility that EF-1 also binds to this site is discussed.

Abrin↗
PubMed1976

Plasmid-determined alcohol dehydrogenase activity in alkane-utilizing strains of Pseudomonas putida.

We have identified an alcohol dehydrogenase activity in Pseudomonas putida strains carrying the CAM-OCT degradative plasmid that were grown on octane. The activity is nicotinamide adenine dinucleotide independent, sediments at 48,000 x g, and shows 20-fold greater activity with octanol rather than butanol as substrate. The enzyme is inducible by unoxidized alkane and is present only in strains that have the OCT plasmid genes for alkane degradation with a wild-type alcO locus. No analogous chromosomal dehydrogenase could be detected. Wild-type and actanol-negative mutants (alcA-) without plasmids both contain a constitutive nicotinamide adenine dinucleotide-linked soluble alcohol dehydrogenase activity. This means that alcA- mutants are cryptic for octanol oxidation and suggests that the particulate plasmid-coded alcohol dehydrogenase activity is active on surface- or membrane-bound substrate.

Alcohol Oxidoreductases↗
PubMed1975

On the mechanism of protein-synthesis inhibition by abrin and ricin. Inhibition of the GTP-hydrolysis site on the 60-S ribosomal subunit.

The mechanism of protein synthesis inhibition by the toxic lectins, abrin and ricin, has been studied in crude and in purified cell-free systems from rabbit reticulocytes and Krebs II ascites cells. In crude systems abrin and ricin strongly inhibited protein synthesis from added aminoacyl-tRNA, demonstrating that the toxins act at some point after the charging of tRNA. Supernatant factors and polysomes washed free of elongation factors were treated separately with the toxins and then neutralizing amounts of anti-toxins were added. Recombination experiments between toxin-treated ribosomes and untreated supernatant factors and vice versa showed that the toxin-treated ribosomes had lost most of their ability to support polyphenylalanine synthesis, whereas treatment of the supernatant factors with the toxins did not inhibit polypeptide synthesis. Recombination experiments between toxin-treated isolated 40-S subunits and untreated 60-S subunits and vice versa showed that only when the 60-S subunits had been treated with the toxins was protein synthesis inhibited in the reconstituted system. The incorporation of [3H]puromycin into nascent peptide chains was unaffected by the toxins, indicating that the peptidyl transferase is not inhibited. Both the EF-1-catalyzed and the EF-2-catalyzed ability of the ribosomes to hydrolyze [gamma-32P]GTP was inhibited by abrin and ricin. An 8-S complex released from the 60-S subunit by EDTA treatment possessed both GTPase and ATPase activity, while the particle remaining after the EDTA treatment had lost most of its GTPase activity. Both enzyme activities of the 8-S complex were inhibited by abrin and ricin. The present data indicate that there is a common site on the 60-S subunits for EF-1- and EF-2- stimulated GTPase activity and they suggest that abrin and ricin inhibit protein synthesis by modifying this site.

Abrin↗
PubMedDate not supplied

Telecommunications and nursing education.

Telecommunications are becoming increasingly important to nursing educators. At the University of Nebraska Medical Center College of Nursing, communication by two-way television, computers, facsimile machines, and telephone conferences is essential to the administration and operation of a school with four divisions located across 500 miles. Two-way television is available through one system that uses satellite and fiberoptic technology and another that uses telephone lines. The four campuses of the college share classes, administrative meetings, and conferences through television. Faculty members teaching via TV are oriented to designing instructional material for transmission and to the minor quirks of the technology. Students in TV classes must be aware of their responsibility for active involvement in learning. Studies have found no significant differences in the grades of students in "live" classrooms and those in TV classrooms, but both faculty and students prefer the face-to-face situation. The College of Nursing uses computers extensively on an internal network linking the four campuses for E-mail, file transfer, computer-assisted instruction, and administrative information sharing. Another computer network, Synapse Health Resources Online, links the college and the Medical Center with health professionals in rural areas throughout the state.

Academic Medical Centers↗
PubMedDate not supplied

Hormone replacement therapy and Alzheimer's disease: an update on the issues.

Alzheimer's disease (AD) is a significant personal, family, social, and public health problem. Currently there is no way to prevent or cure AD. The latest opinions on the possibility of hormone replacement therapy (HRT)/estrogen replacement therapy (ERT) as a means to prevent and treat AD are reviewed. Although prevention and treatment of AD cannot yet be added to the list of HRT/ERT's benefits, research in the area is promising. The potential benefits and problems of HRT for the woman with or at risk for AD are examined. The potential benefits include improved interest and compliance with HRT, improved quality of life, and cost savings. The problems include difficulties in monitoring and managing clients with AD, assuring compliance with the therapeutic regimen, and deciding when to withdraw therapy. Clinical trials have not yet been able to determine the appropriate dosages, to standardize or predict the magnitude of the therapeutic effect, or to determine the safety of ERT/HRT as a long-term therapy, particularly when continued in the elderly years. Implications for practitioners are addressed.

Aged↗