Expression of a chemically synthesized human alpha 1 interferon gene.

Maeyer, Edward De; Skup, Daniel; Prasad, Ketaki Sabnis; Maeyer‐Guignard, Jaqueline De; Williams, B; Meacock, Peter A.; Sharpe, G; Pioli, David; Hennam, J.; Schuch, Wolfgang; Atherton, K. T.

doi:10.1073/pnas.79.14.4256

Cited by 28 publications

(11 citation statements)

References 15 publications

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“…Pure retroviral p24 gag protein was purified from E. coli in a single immunopurification step (Dowbenko et al, 1985) while a five-step process was used to produce human growth hormone (Olsen et al, 1981). Other examples of soluble proteins are human IFN-a (Staehelin et al, 1981;De Maeyer et al, 1982) boVine IFN-a (Grosfeld et al, 1985), chicken triosephosphate isomerase (Straus & Gilbert, 1985), human lymphotoxin (Gray et al, 1984), human TNF (Pennica et al, 1984) and murine TNF .…”

Section: Direct Expressionmentioning

confidence: 99%

The purification of eukaryotic polypeptides synthesized in Escherichia coli

Marston¹

1986

Biochemical Journal

858

379

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Section: Direct Expressionmentioning

confidence: 99%

The purification of eukaryotic polypeptides synthesized in Escherichia coli

Marston¹

1986

Biochemical Journal

858

379

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“…To obtain expression of the sulA gene in E. coli under appropriate conditions but without inducing other SOS functions (including enzymes involved in DNA repair), we inserted a 1.78-kb BamHI fragment from plasmid pTU201 (22) into a position downstream of the lac UV5 promoter of lac expression vector pPM60 (24). This plasmid is derived from pAT153, which has a copy number of 50-60 per cell.…”

Section: Synthesis Of Plasmid-encoded Polypeptides In Maxicelismentioning

confidence: 99%

Role of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells.

Jones¹,

Holland²

1985

Proc. Natl. Acad. Sci. U.S.A.

108

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Induction of the SOS response in Escherichia coli by DNA-damaging treatments results in the synthesis of the SulA polypeptide, and this is sufficient to cause the resulting inhibition of cell division. Mutations at either sul (sfiA) or sudB (sfiB) suppress this division inhibition. The SulB, protein is identical to FtsZ, a protein required for normal division in E. coli. In the presence of FtsZ, the half-life of SulA synthesized in maxicells is -12 min. In contrast, in the absence of FtsZ or in the presence of a mutant form of FtsZ (SulB114) that prevents division inhibition in vivo, SulA is extremely unstable with a half-life of only 3 min. Both FtsZ and SulA are isolated with the inner membrane ofE. coli maxicells in the presence of MgCl2. We propose that the SulA inhibitor interacts directly with FtsZ in vivo to block the essential division function of this protein.The sulB gene, which maps among a cluster of division and related genes at 2 min on the E. coli chromosome, has been postulated by several groups to be the target for the SulA inhibitor. Moreover, in contrast to sulA (11), sulB appears to be part of the normal cell division machinery. We have recently shown (12) that sulBJ14 maps to a locus identical with the ftsZ gene in E. coli. Similarly, Luktenhaus (13) has mapped other sulB alleles (sulB25 and sulB9) toftsZ. TheftsZ gene was shown previously to be essential for cell division in E. coli (14,15). In this study, we used sulA and sulB genes cloned in the same "maxicell" host to obtain evidence for a direct interaction between the SulA and SulB polypeptides. The results obtained indicate that both polypeptides associate with the E. coli inner membrane and that the product of suiB' stabilizes SulA in maxicells.Cell division in UV-irradiated Escherichia coli is initially inhibited and then resumes as DNA repair is completed and blocked replication forks resume elongation. Inhibition of cell division under these conditions was proposed by Witkin (1) to be an inducible function related to recovery from DNA damage. Subsequently, Huisman et al. (2) obtained direct evidence for an inducible inhibitor of division under control of the SOS recA/lexA damage-repair system. In addition, three major classes of mutant affected in this divisioninhibition response have been isolated. Mutations in Ion (3) largely prevent recovery from division inhibition, whereas sulA (sfiA) or sulB (sfMB) mutations (4, 5), which suppress the Lon-phenotype, relieve or reduce division inhibition following DNA damage. However, careful analysis of UV-and nalidixic acid-treated (6) or thymine-starved cells (2) has revealed that division inhibition under these conditions is blocked by at least two independent systems, the "SOS" sulA/suiB pathway and a second pathway which Burton and Holland (6) have suggested is due to failure to terminate DNA replication. Recently, D'Ari and Huisman (7) have reported the presence of a third, sflC-dependent pathway present in some E. coli K-12 strains. In this paper, we are concerned specifically...

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“…Subsequent work led to the expression in M. methylotrophus of the chicken ovalbumin and mouse dihydrofolate reductase genes, 219 and of a chemically synthesized human al interferon gene. 220 These results were originally made possible by the development of small, high-copy-number, wide-host-range plasmids, and similar vectors may find use in other SCP-quality microorganisms. The excellent results reported in these studies with M. methylotrophus are very encouraging in that they allow us to envision the near-term, industrial-scale use of SCP organisms with a high level of wholesome protein that coproduce high-value products such as fine chemicals and pharmaceuticals.…”

Section: B Protoplast Fusionmentioning

confidence: 99%

Single‐cell protein: Current status and future prospects

Tusé

1983

C R C Critical Reviews in Food Science and Nutrition

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The consumption of microorganisms by man and animals is not a revolutionary new idea. For thousands of years man has consumed, either intentionally or unintentionally, such products as alcoholic beverages, cheeses, yogurt, and soya sauce and, along with these products, the microbial biomass responsible for their production. The rapid growth rate and high protein content of microbes and their ability to utilize inexpensive feedstocks as sources of carbon and energy for growth have made microorganisms prime candidates for use as human food and animal feed protein supplements. Yet, in spite of their promise, only a limited number of commercial-scale, single-cell protein (SCP) processes have been seen. Recently, with the advent of recombinant DNA technology a rebirth of interest in SCP has resulted. This review analyzes the answers to two questions: (1) how far have we come?; and (2) what impact, if any, will the new biotechnologies have in this field?

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Expression of a chemically synthesized human alpha 1 interferon gene.

Cited by 28 publications

References 15 publications

The purification of eukaryotic polypeptides synthesized in Escherichia coli

The purification of eukaryotic polypeptides synthesized in Escherichia coli

Role of the SulB (FtsZ) protein in division inhibition during the SOS response in Escherichia coli: FtsZ stabilizes the inhibitor SulA in maxicells.

Single‐cell protein: Current status and future prospects

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