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  • 1
    Electronic Resource
    Electronic Resource
    Liberation of Tyrosine Hydroxyl Groups in Urea Solutions of Bovine Serum Albumin and Ovalbumin (1957)
    [s.l.] : Nature Publishing Group
    Nature 180 (1957), S. 1286-1287 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The spectrum (above 255 m^) of aqueous solutions of bovine serum albumin was found to be essentially independent of pH. over the range 4'4-8-0 in the absence of urea. However, when the pH was adj usted to less than 4-4, the absorption peak at 279 TS\\L shifted instantaneously to lower wave-lengths ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1801286a0
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution (1955)
    [s.l.] : Nature Publishing Group
    Nature 176 (1955), S. 738-738 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] During the past three years, a physicochemical study has been made in this laboratory of proteins in urea solution. Observations on sedimentation and diffusion for ovalbumin and bovine serum albumin are briefly reported here. Data for the denaturation of 1 per cent (w/v) protein in 7 M urea (with ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/176738a0
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  • 3
    Electronic Resource
    Electronic Resource
    Protein–nucleoside contacts in the interaction between the replication terminator protein of Bacillus subtilis and the DNA terminator (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The interaction between the DNA replication terminator, IRI, of Bacillus subtilis and its cognate replication terminator protein (RTP) has been examined by the technique of missing nucleoside interference (MNI). IRI contains two adjacent binding sites (A and B) for RTP dimers. The B site is proximal to the replication fork arrest site. The present results have shown that nucleoside contacts with RTP in the two sites are very different. There are more extensive contacts of nucleosides in both strands of the B site with RTP compared with the A site. The data also strongly suggest that filling by RTP of the B site occurs first and is needed for subsequent co-operative filling of an overlapping A site. The A site alone binds RTP poorly. The findings are consistent with interaction occurring between RTP dimers bound to adjacent sites of IRI, which would explain why RTP bound to the B site alone cannot cause replication fork arrest.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb00947.x
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  • 4
    Electronic Resource
    Electronic Resource
    Functional specificity of the replication fork-arrest complexes of Bacillus subtilis and Escherichia coli: significant specificity for Tus–Ter functioning in E. coli (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 36 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Escherichia coli replication terminator TerB was inserted in its two alternate orientations into a Bacillus subtilis fork-arrest assay plasmid. After transferring these new plasmids into B. subtilis, which could overproduce the E. coli terminator protein Tus, it was shown that the E. coli Tus–TerB complex could cause polar replication fork arrest, albeit at a very low level, in B. subtilis. A new B. subtilis–E. coli shuttle plasmid was designed to allow the insertion of either the TerI (B. subtilis) or TerB (E. coli) terminator at the same site and in the active orientation in relation to the approaching replication fork generated in either organism. Fork-arrest assays for both terminator-containing plasmids replicating in both organisms which also produced saturating levels of either the B. subtilis terminator protein (RTP) or Tus were performed. The efficiency of the Tus–TerB complex in causing fork arrest was much higher in E. coli than in B. subtilis. The efficiency of the B. subtilis RTP–TerI complex was higher in B. subtilis than in E. coli, but the effect was significantly less. Evidently a specificity feature in E. coli operates to enhance appreciably the fork-arrest efficiency of a Tus–Ter complex. The specificity effect is of less significance for an RTP–Ter complex functioning in B. subtilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01945.x
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  • 5
    Electronic Resource
    Electronic Resource
    Characterization of the essential cell division gene ftsL (yllD ) of Bacillus subtilis and its role in the assembly of the division apparatus (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 29 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have identified the Bacillus subtilis homologue of the essential cell division gene, ftsL, of Escherichia coli. Repression of ftsL in a strain engineered to carry a conditional promoter results in cell filamentation, with a near immediate arrest of cell division. The filaments show no sign of invagination, indicating that division is blocked at an early stage. FtsL is also shown to be required for septation during sporulation, and depletion of FtsL blocks the activation but not the synthesis of the prespore-specific sigma factor, σF. Immunofluorescence microscopy shows that depletion of FtsL has little or no effect on FtsZ ring formation, but the assembly of other division proteins, DivIB and DivIC, at the site of division is prevented. Repression of FtsL also results in a rapid loss of DivIC protein, indicating that DivIC stability is dependent on the presence of FtsL, in turn suggesting that FtsL is intrinsically unstable. The instability of one or more components of the division apparatus may be important for the cyclic assembly/disassembly of the division apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00954.x
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  • 6
    Electronic Resource
    Electronic Resource
    DivIB, FtsZ and cell division in Bacillus subtilis (1997)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 23 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Bacillus subtilis cell-division protein DivIB is shown to be present at an ≈100-fold higher abundance (≈5000 molecules per cell) than its Escherichia coli FtsQ homologue. B. subtilis contains much more DivIB (at least 60-fold) than is needed to maintain the normal rate of cell division at moderate temperatures (up to 37°C). However, a high level of DivIB is needed to achieve the normal rate of division at high temperature (47°C). It is proposed that membrane-bound DivIB is involved in stabilizing or promoting the assembly of the division complex (which is intrinsically temperature sensitive) in a manner that requires more of the protein at higher temperatures. The (at least) 60-fold accumulation of DivIB and FtsZ from an undetectable level, following germination and outgrowth of spores up until the stage of the first cell division, was unaffected by blocking of initiation of the first round of replication. It is concluded that there is no major synthesis of either of these ‘division initiation’ proteins linked to initiation, progression or completion of the first round of replication accompanying spore outgrowth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.2141580.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of mutations in divlB of Bacillus subtilis and cellular localization of the DivlB protein (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 7 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Four temperature-sensitive mutations in the divlB gene of Bacillus subtilis have been localized to the region corresponding to the C-terminal half of the 263-residue DivlB protein. Antiserum was raised to the 80%C-terminal portion lying on one side of a putative transmembrane (hydrophobic) segment, and used to examine aspects of the nature and localization of the DivIB protein in the cell. A single DivIB species of a size equal to the full-length protein encoded by the divIB gene was detected in wild-type cells. Cell fractionation studies established that DivIB is associated preferentially with the cell envelope (membrane plus cell wall), with approximately 50% being released into solution upon treatment of cells with lysozyme under conditions that yield protoplasts. Of the remaining 50%, approximately half remained firmly associated with the membrane fraction. On the basis of the‘positive-inside rule’of von Heijne (1986) it is suggested that the topology of membrane-bound DivlB is such that the long C-terminal portion is directed to the outside and the smaller N-terminal portion to the inside of the cell. DivlB in protoplasts was rapidly degraded by proteinase K under conditions where there was no general proteolysis of the cytoplasmic proteins. This is consistent with its absence from the cytoplasm, and with the predicted membrane topology.Septum positioning in a divIB null mutant, which grows as filaments at temperatures of 30°C and below, was found to be normal. It appears that DivlB is needed for achieving the appropriate rate of initiation of septum formation at normal division sites. It is proposed that the C-terminal portion of DivlB, localized on the exterior surface of the membrane and in juxtaposition to the peptidoglycan, normally interacts with another protein (or proteins) to initiate septum formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01152.x
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  • 8
    Electronic Resource
    Electronic Resource
    Amphiphile Nature of κ-Casein as the Basis for its Micelle Stabilizing Property (1969)
    [s.l.] : Nature Publishing Group
    Nature 221 (1969), S. 635-639 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The N-terminal two-thirds of the milk micelle stabilizer κ-casein are hydrophobic and the C-terminal third is hydrophilic; the protein is an amphiphile. The two regions may function respectively to anchor the κ-casein molecule to the hydrophobic calcium ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/221635a0
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  • 9
    Electronic Resource
    Electronic Resource
    Tussle with a terminator (1996)
    [s.l.] : Nature Publishing Group
    Nature 383 (1996), S. 582-583 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] TOWARDS the end of a round of replication of a circular bacterial chromosome, two approaching replication forks are forced to meet within a restricted 'terminus' region, approximately opposite the origin. This is achieved through the presence of a replication-fork arrest system in this region (Fig. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/383582a0
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  • 10
    Electronic Resource
    Electronic Resource
    Chromosome Partitioning in Bacteria (1995)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 29 (1995), S. 41-67 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ge.29.120195.000353
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