Molecular and Genetic Studies of an R Factor System Consisting of Independent Transfer and Drug Resistance Plasmids

Embden, Jan Van; Cohen, Stanley N.

doi:10.1128/jb.116.2.699-709.1973

Cited by 57 publications

(25 citation statements)

References 44 publications

(60 reference statements)

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“…General cloning techniques were carried out essentially as described by Maniatis et al (Maniatis et al, 1982). Plasmid DNA was isolated from E. coli by the cleared-lysate method (Van Embden and Cohen, 1973) and purified by using Qiagen. For rapid screening, plasmid DNA was isolated by the alkaline lysis method (Maniatis et al, 1982).…”

Section: Dna Manipulationsmentioning

confidence: 99%

Expression of the Mau Genes Involved in Methylamine Metabolism in Paracoccus denitrificans is Under Control of a LysR-type Transcriptional Activator

Spanning¹,

Palen²,

Slotboom³

et al. 1994

Eur J Biochem

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Expression of methylamine dehydrogenase in Paracoccus denitrificans and its concomitant ability to grow on methylamine is regulated by a substrate-induction mechanism as well as by a catabolite-repression-like mechanism. Methylamine dehydrogenase is synthesized in cells growing on either methylamine or ethylamine, but not during growth on succinate, methanol or choline as sole sources of carbon and energy. The synthesis of methylamine dehydrogenase is repressed when succinate is added to the growth medium in addition to methylamine. Repression is not observed when the growth medium contains methylamine and either choline or methanol. Induction of the mau genes encoding methylamine dehydrogenase is under control of the mauR gene. This regulatory gene is located directly in front of, but with the transcription direction opposite to that of, the structural genes in the mau cluster. The mauR gene encodes a LysR-type transcriptional activator. Inactivation of the gene results in loss of the ability to synthesize methylamine dehydrogenase and amicyanin, and loss of the ability to grow on methylamine. The mutation is completely restored when the mauR gene is supplied in trans. The first gene of the cluster of mau genes that is under control of MauR is mauF, which encodes a putative membrane-embedded protein. Inactivation of the gene results in the inability of cells to grow on methylamine. Downstream from mauF and in the same transcription direction, mauB is located. This gene encodes the large subunit of methylamine dehydrogenase.

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Section: Dna Manipulationsmentioning

confidence: 99%

Expression of the Mau Genes Involved in Methylamine Metabolism in Paracoccus denitrificans is Under Control of a LysR-type Transcriptional Activator

Spanning¹,

Palen²,

Slotboom³

et al. 1994

Eur J Biochem

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“…Plasmid DNA was isolated by the cleared-lysate method [11] followed by CsCl-ethidium bromide density-gradient centrifugation. Double-stranded DNA from M13 recombinant phages was isolated from 1-ml cultures by the lysozyme-boiling method [121.…”

Section: Dna Sequence Analysismentioning

confidence: 99%

Characterization of the pColV-K30 encoded cloacin DF13/aerobactin outer membrane receptor protein of Escherichia coli; isolation and purification of the protein and analysis of its nucleotide sequence and primary structure

Krone

1985

FEMS Microbiology Letters

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The cloacin DF13/aerobactin receptor protein from Escherichia coli (pFS8) and from Klebsiella edwardsii were isolated by repeated Triton X-100 extractions and purified by affinity chromatography. Both receptor proteins ran as a single protein band on SDS-PAGE. Their apparent M r values were 74000 and 76 000, respectively. The binding constants of the purified receptor proteins from E. coli (pFS8) and K. edwardsii and cloaein DF13 were determined. Values of 2.0 × 10 s M -1 and 1.0 x 109 M -1, respectively, were found.The nucleotide sequence of the pColV-K30 gene, contained on pFS8 and encoding the cloacin DF13/aerobactin receptor protein, was determined and the primary structure of the protein as well as its secondary structure were deduced. The results revealed that the pColV-K30-specified receptor protein might be synthesized as a precursor, with a signal sequence of 25 amino acid residues. The mature protein has an M r of 77 345.

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“…Plasmid DNA was isolated by the cleared-lysate method [4] followed by CsCl ethidium bromide density-gradient centrifugation. Double-strand DNA (dsDNA) from Ml3 recombinant phages was isolated from l-ml cultures by the lysozyme boiling method [5].…”

Section: Isolation Of Plasmid and Ml3 Dsdnamentioning

confidence: 99%

The nucleotide sequence of the gene encoding the K99 subunit of enterotoxigenic Escherichia coli

Roosendaal

1984

FEMS Microbiology Letters

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The nucleotide sequence of the gene encoding the K99 fimbrial subunit of enterotoxigenic Escherichia coli was determined. It appeared that the subunit is composed of 159 amino acid residues preceded by a N-terminal signal sequence of 22 amino acid residues. The secondary structure of the mature K99 polypeptide and the location of potential antigenic determinants were predicted. A comparison was made between the amino acid sequence of the K99 subunit and the subunits of other fimbrial adhesins.

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Molecular and Genetic Studies of an R Factor System Consisting of Independent Transfer and Drug Resistance Plasmids

Cited by 57 publications

References 44 publications

Expression of the Mau Genes Involved in Methylamine Metabolism in Paracoccus denitrificans is Under Control of a LysR-type Transcriptional Activator

Expression of the Mau Genes Involved in Methylamine Metabolism in Paracoccus denitrificans is Under Control of a LysR-type Transcriptional Activator

Characterization of the pColV-K30 encoded cloacin DF13/aerobactin outer membrane receptor protein of Escherichia coli; isolation and purification of the protein and analysis of its nucleotide sequence and primary structure

The nucleotide sequence of the gene encoding the K99 subunit of enterotoxigenic Escherichia coli

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