Lactobacillus casei phage PL-1 Molecular properties and first transcription studies in vivo and in vitro

Stetter, Karl O.; Priess, Harro; Delius, Hajo

doi:10.1016/0042-6822(78)90152-6

Cited by 30 publications

(23 citation statements)

References 34 publications

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“…1 c), phage PL-} had an isometric head of 54 ± 3 nm, a non-contractile tail of 262 ± 4 nm x 9 ± 2 nm, a baseplate 14 ± 1 nm X 7 ± 2 nm, a tail fiber 69 ± 3 nm, and the tail consisted of 68 discs. These are approximately the same results as those reported by Stetter et al 20 ) and by Watanabe etal. 2l )…”

Section: Morphology Of Phages Lc-nu Pl-l and L/>fswsupporting

confidence: 83%

“…The PL-I genome was 38.1 kb, based on the sizes of restriction fragments from EcoRI, HindUI, BamHI-EcoRI, and Sall-EcoRI digestions. Stetter et al 20 ) have reported similar sizes of EcoRI fragments for PL-l as we obtained in this study. The comparison of the restriction patte'rns of LC-Nu, PL-l, and c/>FSW (e.g., BamHI and Sail digestions) found no significant similarities.…”

Section: Organization Of Phage Genomessupporting

confidence: 79%

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Structural Similarity and Genetic Homology betweenLactobacillus caseiBacteriophages Isolated in Japan and in Finland

Forsman

Tanskanen

Alatossava

1993

Bioscience, Biotechnology, and Biochemistry

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Section: Morphology Of Phages Lc-nu Pl-l and L/>fswsupporting

confidence: 83%

Section: Organization Of Phage Genomessupporting

confidence: 79%

Structural Similarity and Genetic Homology betweenLactobacillus caseiBacteriophages Isolated in Japan and in Finland

Forsman

Tanskanen

Alatossava

1993

Bioscience, Biotechnology, and Biochemistry

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“…Poly[d(A-T)] was obtained from Boehringer (Mannheim). Bacteriophage DNAs were obtained as described by Stetter et al [9]. Single-stranded DNA was prepared by alkaline denaturation [lo] of commercial native calf thymus DNA (Sigma, St Louis) purified additionally by phenol extractions and centrifugations in a CsCl gradient.…”

Section: Materials a N D Methodsmentioning

confidence: 99%

DNA-dependent RNA polymerase from the extremely halophilic archaebacterium Halococcus morrhuae

1983

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Pure and absolutely DNA-dependent RNA polymerase has been isolated from the extremely halophilic archaebacterium, Halococcus rnorrhuae. It is composed of five heavy (1 42 000; 88 000; 73 000; 52 500; and 49 500 Da) and five small components (13 300; 11 200; 10 800; 10 500; 9900 Da). The peptides of 49 500 D a and 52500 D a probably represent one component in different modification states.Single-stranded DNA shows the highest template efficiency, although archaebacterial chromosomal DNAs are efficiently transcribed.Rifampicin, streptolydigin and sc-amanitin do n o t inhibit transcription by this enzyme. Heparin permits elongation but not initiation of transcription.The activity of H . rnorrliuac~ RNA polymerase is strongly stimulated by glycerol and dimethylsulfoxide.The component patterns of RNA polymerases of archaebacteria [I] are one of many features distinguishing these organisms from eubacteria [2]. Their complexity resembles that of the patterns of eukaryotic RNA polymerases [2].For comparative analysis of their structures, RNA polymerases have been isolated from all orders of the two branches [3] of the urkingdom of archaebacteria [2,4,5]. The Halohacreriales, however, were only represented by the polymerase from Halobacterium lzulobiurn [6]. The isolation of an enzyme from the genus Halococcus, representing another family of this order, appeared useful for determining the phylogeny within the group because Halococcus differs markedly from Halobacterium in many other respects, e.g. in the nature of its envelope [7] and in 16s rRNA sequence [3,81. In this paper we describe the purification, the composition and some enzymic properties of the RNA polymerase of Halococcus morrhuae. We focused our attention on the comparison of this enzyme with those from H . hulobiun~ and other archaebacteria. MATERIALS A N D METHODSHalococcus morrizuae, strain CCM 531 (neotype Vulcani), was grown at 37' C and pH 7.3 ~ 7.5. Thc medium contained in 1 I : 230g NaCI, 5 g MgS04. 7H,O, 1 g KCI, 0.15g CaC12. 2 H 2 0 , 5 g Tryptone (Oxoid) and 5 g yeast extract (Difco).AhDrevintioirs. SDS, sodium dodecylsulfale; MeZSO, dimethylsulfoxide.En;j,me. R N A nucleotidyltransferase or DNA-dependent RNA polymerase, nucleosidetriphosphate: R N A nucleotidyltransferase (EC 2.7.7.6).Purjfi'critio,z of R N A poljwrra.ve 100 g frozen cells were suspended in 250 ml buffer containing 0.05 M Tris/acetate, pH 7.5, 0.05 M MgC12, 0.005 M 2-mercaptoethanol, 0.001 M EDTA, 0.002 M phenylmethylsulfonyl fluoride and 407; glycerol and disrupted in the French press at a pressure of 131 MPa. An additional 250-ml aliquot of the same buffer was added to the homogenate and the suspension was mixed thorougly.For the further purification of H . morrliuae polymerase the method previously described for Halobacterium halohium RNA polymerase [6] was followed.

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“…Bacteriophage DNAs were isolated by phenol extraction [7]. Poly [d(A-T)] was obtained from Boehringer (Mannheim).…”

Section: __ ~~~~mentioning

confidence: 99%

A Form of the DNA‐Dependent RNA Polymerase of Halobacterium halobium, Containing an Additional Component, Is Able to Transcribe Native DNA

Madon

Zillig

1983

European Journal of Biochemistry

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A revised procedure for the purification of DNA-dependent RNA polymerase from Halobacterium halohiurn, including two-phase partition, yields pure, highly active and absolutely DNA-dependent enzyme. Two forms of the enzyme, one containing, the other not containing a previously not observed component, E , show striking differences in activity. RNA polymerase without component E has a significant activity on poly[d(A-T)] but only insignificant activity on all other templates. The enzyme containing a stoichiometric amount of component E transcribes poly [d(A-T)] and native templates efficiently.A method for the purification of the DNA-dependent RN A polymerase of Halobacterium halohiurn and some properties of the enzyme have been described previously [l]. Aside from being unable to initiate transcription at high ionic strength, the RNA polymerase isolated in this way was not completely dependent on added DNA, probably as a consequence of its content of small DNA fragments resulting from the use of DNase in removing endogenous DNA. Moreover, this enzyme though very active on single-stranded DNA and poly [d(A-T)] was almost inactive on native DNAs.We here describe modifications of the previous method, which allow the isolation of an enzyme absolutely free of endogenous DNA and thus completely dependent on the addition of template and containing a previously unobserved component required for transcription. This enzyme is able to transcribe native DNA with reasonable efficiency. MATERIALS AND METHODS Purijkation of R N A PolymeraseHalobacterium Iiulobium, strain WT, was grown as described by Oesterhelt and Stoeckenius [2].The previously described method for the isolation of DNAdependent RNA polymerase [I] was modified as follows. To 100 g frozen bacteria 500 ml buffer A (0.05 M Tris/acetate, pH 7.5, 0.05 M MgCI,, 0.005 M 2-mercaptoethanol, 0.001 M EDTA, 0.002 M phenylmethylsulfonyl fluoride (PhMeS02F) and 40 % glycerol) were added. The bacteria were rapidly thawed in a 37 "C water bath, then quickly cooled in ice and homogenized by means of an Ultraturrax homogenizer. The separation of the RNA polymerase from the DNA and a first purification were achieved by adaptation of the two-phase partition method first used by Babinet for RNA polymerase preparation Enzyme. RNA nucieotidyltransferase or DNA-dependent RNA polymerase, nucleosidetriphosphate : RNA nucleotidyltransferase (EC 2.7.7.6).poly(ethyleneglyco1) (PEG 20000, Serva, Heidelberg) in buffer A were added to the homogenate. The suspension was stirred for 30 min in an ice bath. The separation of the phases was performed by centrifugation for 20 min at 10000 rev./min, 2 "C, in the JA-10 rotor of the Beckman J-21B centrifuge. The upper (PEG) phase was carefully decanted. The lower (dextran) phase was mixed with 370 ml buffer B (buffer A without glycerol) by means of the Ultraturrax homogenizer. To this mixture 150 ml30 % PEG and 53 g solid NaCl were added and the suspension was stirred for 30 min. The separation ofphases was achieved as above. The PEG phase was again di...

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Lactobacillus casei phage PL-1 Molecular properties and first transcription studies in vivo and in vitro

Cited by 30 publications

References 34 publications

Structural Similarity and Genetic Homology betweenLactobacillus caseiBacteriophages Isolated in Japan and in Finland

Structural Similarity and Genetic Homology betweenLactobacillus caseiBacteriophages Isolated in Japan and in Finland

DNA-dependent RNA polymerase from the extremely halophilic archaebacterium Halococcus morrhuae

A Form of the DNA‐Dependent RNA Polymerase of Halobacterium halobium, Containing an Additional Component, Is Able to Transcribe Native DNA

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