DNA Restriction Enzyme from E. coli

Meselson, Matthew; Yuan, Robert

doi:10.1038/2171110a0

Cited by 742 publications

(261 citation statements)

References 23 publications

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“…CC118.1 is a derivative of CC118 (Manoil and Beckwith, 1985) that contains FЈ lacI q1 lacZ ::Tn5; it was used as a host strain for the B. burgdorferi genomic library and identification of clones expressing haemolytic activity. E. coli MM294 (Meselson and Yuan, 1968) was routinely used as the host strain for pDP1 and its derivatives; DH5␣ (Raleigh et al, 1988) was used routinely for plasmid DNA manipulation; and BL21(DE3), BL21(DE3)(pLysE), BL21(DE3)(pLysS) (Studier et al, 1990), and MM294(DE3) (this work) were used for expression of plasmids containing the T7 promoter. Plasmid pET11b (Studier et al, 1990) was used for cloning and expression of blyA and blyB.…”

Section: Methodsmentioning

confidence: 99%

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Guina

Oliver

1997

Molecular Microbiology

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SummaryWe cloned the gene encoding a membrane-interactive protein of Borrelia burgdorferi by means of its haemolytic activity in Escherichia coli. The haemolytic activity was erythrocyte-species specific, with progressively decreasing activity for erythrocytes from horse, sheep, and rabbit, respectively. Genetic analysis of the haemolytic determinant revealed two borrelia haemolysin genes, blyA and blyB, that are part of a predicted four-gene operon which is present in multiple copies on the 30 kb circular plasmid(s) of B. burgdorferi B31. blyA encodes a predicted ␣-helical 7.4 kDa protein with a hydrophobic central region and a positively charged C-terminus, which is structurally homologous to a large group of pore-forming toxins with cytolytic activity. blyB encodes a soluble protein which stabilized BlyA and enhanced haemolytic activity. While the majority of BlyA in E. coli was membrane-associated, only soluble protein was haemolytically active. The haemolytic activity was shown to be highly protease sensitive, heat labile, independent of divalent cations, and extremely dependent on protein concentration, consistent with a requirement for oligomerization as the mechanism of action. BlyA was highly purified from E. coli in a single step utilizing Triton X-114 phase partitioning. Genetic analysis of blyA and blyB mutants indicated that the stability, membrane association, and activity of BlyA was dependent on subtle changes in its sequence and on the BlyB protein. The bly genes were found to be expressed at a very low level in cultured B. burgdorferi.

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Section: Methodsmentioning

confidence: 99%

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Guina

Oliver

1997

Molecular Microbiology

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“…The first evidence for this discriminatory process was the demonstration of a barrier, albeit incomplete, to the productive infection of Escherichia coli strain K-12 by bacteriophage λ previously propagated in either E. coli strain C or E. coli strain B (Bertani & Weigle, 1953). Much later it was proven that the growth of phages in E. coli K-12 can be ' restricted ' by an endonuclease, a restriction enzyme (EcoKI), which attacks foreign DNA (Meselson & Yuan, 1968 ;Linn & Arber et al, 1969). Occasionally phages escape restriction and they, like the resident bacterial chromosome, acquire a protective identification mark from a strain-specific modification enzyme that methylates defined bases within a specific target sequence (Arber & Dussoix, 1962 ;Smith et al, 1972).…”

Section: Background and Aimsmentioning

confidence: 99%

Immigration control of DNA in bacteria: self versus non-self

Murray¹

2002

Microbiology

153

143

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“…Neomycin and puromycin have been used as co-selection markers before (Wirth et al, 1988). All plasmids were propagated in Escherichia coli DH1 (Low, 1968;Meselson and Yuan, 1968) and were purified by cesium chloride gradient centrifugation.…”

Section: Plasmidsmentioning

confidence: 99%

A Unique Autophosphorylation Site in the Platelet‐Derived Growth Factor α Receptor from a Heterodimeric Receptor Complex

Rupp

Siegbahn

Rönnstrand

et al. 1994

European Journal of Biochemistry

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The platelet-derived growth factor (PDGF) a and p receptors undergo dimerization as a consequence of ligand binding. Depending on the PDGF isoform (PDGF-AA, -AB or -BB), homodimers or heterodimers of receptors are formed. In this study, we have used transfected porcine aortic endothelial cells, coexpressing cDNAs for the a receptor and the p receptor at comparable levels, to investigate the properties of the up-heterodimeric receptor complex. PDGF-AB, which mainly induced ap-heterodimeric complexes, was the most efficient isoform for stimulating mitogenicity. Actin reorganization, in the form of circular membrane ruffling and chemotaxis, was induced by PDGF-AB and PDGF-BB, but not by PDGF-AA, thus indicating that the p receptor in the homodimeric or heterodimeric configuration was required for induction of motility responses. The molecular basis for the apparent receptor dimer-specific properties was examined by analyzing receptor autophosphorylation and phosphorylation of substrates. The a receptor was found to be phosphorylated at an additional tyrosine residue, Tyr754, in the heterodimeric complex as compared to the aa receptor homodimer. Phosphorylation of this tyrosine residue could permit the binding of a specific signal-tranducing protein. A candidate is a 134000-Mr protein, which was shown to associate preferentially with the a receptor in the heterodimeric receptor complex. It is possible that phosphorylated Tyr754 in the a receptor mediates activation of specific signal-tranducing molecules like the 134 000-M, substrate, and thereby initiates signal-tranduction pathways from the ap receptor heterodimer, which are distinct from those initiated via homodimeric receptor complexes.

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DNA Restriction Enzyme from E. coli

Cited by 742 publications

References 23 publications

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Cloning and analysis of a Borrelia burgdorferi membrane‐interactive protein exhibiting haemolytic activity

Immigration control of DNA in bacteria: self versus non-self

A Unique Autophosphorylation Site in the Platelet‐Derived Growth Factor α Receptor from a Heterodimeric Receptor Complex

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