Richard Bass

Virginia Commonwealth University

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Ellis Englesberg

University of California, Santa Barbara

Laurel Heffernan

University of California, Los Angeles

Larry E. Dillehay

Johns Hopkins Medicine

Gail E. Christie

Virginia Commonwealth University

Gary Wilcox

UNSW Sydney

Pierre Meuris

University of California, Los Angeles

John R. Moffett

Uniformed Services University of the Health Sciences

H B Hedegaard

Jewish Hospital

S M Cuskey

Craft Engineering Associates (United States)

Nydia M. Morales

Virginia Commonwealth University

Cooperative Institutions

University of California, Santa Barbara

Virginia Commonwealth University

Virginia Commonwealth University Medical Center

University of California, Los Angeles

Jewish Hospital

Lawrence Livermore National Laboratory

University of Michigan–Ann Arbor

East Carolina University

John Wiley & Sons (United States)

Hudson Institute

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Inhibition of the growth of mammalian cells in culture by amino acids and the isolation and characterization ofL-phenylalanine-resistant mutants modifyingL-phenylalanine transport

Somatic Cell Genetics (1976)

Ellis Englesberg Richard Bass William C. Heiser

10.1007/bf01542722

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Citations (38)

Regulation of the l-Arabinose Operon BAD in Vitro

Journal of Biological Chemistry (1974)

Gary Wilcox Pierre Meuris Richard Bass Ellis Englesberg

Abstract A DNA-directed cell-free system to study the l-arabinose BAD operon has been further developed so that the rate of synthesis of enzymes coded for by the structural genes in the operon in vitro is about 5% the in vivo rate. l-Arabinose isomerase and l-ribulokinase, the products of the araA and araB genes, are synthesized at the same rate, demonstrating that the operon is coordinately expressed in vitro. The system is completely dependent upon araC protein which can be supplied either by synthesis in vitro from an araC+ DNA template or by the addition of araC protein extracted from whole cells. The properties in the in vitro system of araC protein from either source suggests that the two products are similar if not identical. Both the repressor and activator forms of the araC protein are demonstrable in vitro using the appropriate templates confirming the essential aspects of the model for gene regulation of this operon.

L-arabinose operon

gal operon

Arabinose

10.1016/s0021-9258(19)42723-3

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Citations (73)

The A, ASC, and L systems for the transport of amino acids in Chinese hamster ovary cells (CHO-K1).

Journal of Biological Chemistry (1981)

Richard Bass H B Hedegaard Larry E. Dillehay John R. Moffett Ellis Englesberg

10.1016/s0021-9258(19)68613-8

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Citations (61)

Elucidation of an a and L system for amino acid transport in the human lymphoblast using a membrane filtration technique

In Vitro (1979)

Richard Bass Ellis Englesberg

Filtration (mathematics)

Lymphoblast

Alanine

Membrane filter

10.1007/bf02618310

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Citations (11)

Mutations affecting catabolite repression of the L-arabinose regulon in Escherichia coli B/r

Journal of Bacteriology (1976)

Laurel Heffernan Richard Bass Ellis Englesberg

Expression of the L-arabinose regulon in Escherichia coli B/r requires, among other things, cyclic adenosine-3', 5'-monophosphate (cAMP) and the cAMP receptor protein (CRP). Mutants deficient in adenyl cyclase (cya-), the enzyme which synthesizes cAMP, or CRP (crp-) are unable to utilize a variety of carbohydrates, including L-arabinose. Ara+ revertants of a cya-crp- strain were isolated on 0.2% minimal L-arabinose plates, conditions which require the entire ara regulon to be activated in the absence of cAMP and CRP. Evidence from genetic and physiological studies is consistent with placing these mutations in the araC regulatory gene. Deletion mapping with one mutant localized the site within either araO or araC, and complementation tests indicated the mutants acted trans to confer the ability to utilize L-arabinose in a cya-crp- genetic background. Since genetic analysis supports the conclusion, that the mutant sites are in the araC regulatory gene, the mutants were designated araCi, indicating a mutation in the regulatory gene affecting the cAMP-CRP requirement. Physiological analysis of one mutant, araCi1, illustrates the trans-acting nature of the mutation. In a cya-crp- genetic background, araCi1 promoted synthesis of both isomerase, a product of the araBAD operon, and permease, a product of the araE operon. Isomerase and permease levels in araCi1 cya+ crp+ were hyperinducible, and the sensitivity of each to cAMP was altered. Two models are presented that show the possible mutational lesion in the araCi strains.

Regulon

L-arabinose operon

PEP group translocation

10.1128/jb.126.3.1119-1131.1976

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Citations (36)

Analysis of cloned structural and regulatory genes for carbohydrate utilization in Pseudomonas aeruginosa PAO

Journal of Bacteriology (1990)

Louise Temple S M Cuskey R.E. Perkins Richard Bass Nydia M. Morales

Five of the genes required for phosphorylative catabolism of glucose in Pseudomonas aeruginosa were ordered on two different chromosomal fragments. Analysis of a previously isolated 6.0-kb EcoRI fragment containing three structural genes showed that the genes were present on a 4.6-kb fragment in the order glucose-binding protein (gltB)-glucokinase (glk)-6-phosphogluconate dehydratase (edd). Two genes, glucose-6-phosphate dehydrogenase (zwf) and 2-keto-3-deoxy-6-phosphogluconate aldolase (eda), shown by transductional analysis to be linked to gltB and edd, were cloned on a separate 11-kb BamHI chromosomal DNA fragment and then subcloned and ordered on a 7-kb fragment. The 6.0-kb EcoRI fragment had been shown to complement a regulatory mutation, hexR, which caused noninducibility of four glucose catabolic enzymes. In this study, hexR was mapped coincident with edd. A second regulatory function, hexC, was cloned within a 0.6-kb fragment contiguous to the edd gene but containing none of the structural genes. The phenotypic effect of the hexC locus, when present on a multicopy plasmid, was elevated expression of glucokinase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydratase, and 2-keto-3-deoxy-6-phosphogluconate aldolase activities in the absence of inducer.

Structural gene

Glucokinase

Phosphogluconate dehydrogenase

10.1128/jb.172.11.6396-6402.1990

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Citations (25)

The site for catabolite deactivation in the L-arabinose BAD operon in Escherichia coli B/r

Archives of Microbiology (1976)

Richard Bass Laurel Heffernan Katherine Sweadner Ellis Englesberg

Derepression

Transcription

L-arabinose operon

Fed-batch culture

trp operon

10.1007/bf00416978

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Citations (11)

Inhibition of growth of cells in culture by L‐phenylalanine as a model system for the analysis of phenylketonuria. I. Amino acid antagonism and the inhibition of protein synthesis

Journal of Cellular Physiology (1980)

Larry E. Dillehay Richard Bass Ellis Englesberg

Abstract Phenylalanine in high concentrations inhibits the growth of mouse A9 cells. Protein synthesis is inhibited earlier and more severely than RNA or DNA synthesis. Phenylalanine inhibits the uptake and decreases the intracellular pool of several amino acids. Certain amino acids added in excess reverse the phenylalanine inhibition. The strongest reversing amino acids appear to function by excluding phenylalanine. The phenylalanine inhibition does not appear to be due to a deficiency of any amino acid, but to the high intracellular phenylalanine concentration and/or an amino acid imbalance resulting from the large ratio of phenylalanine to other amino acids.

Phenylalanine hydroxylase

10.1002/jcp.1041020314

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Citations (6)