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  • 11
    Electronic Resource
    Electronic Resource
    Antagonistic effects of dual PTS-catalysed phosphorylation on the Bacillus subtilis transcriptional activator LevR (1998)
    Oxford BSL : Blackwell Science Ltd, UK
    Molecular microbiology 28 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: LevR, which controls the expression of the lev operon of Bacillus subtilis, is a regulatory protein containing an N-terminal domain similar to the NifA/NtrC transcriptional activator family and a C-terminal domain similar to the regulatory part of bacterial anti-terminators, such as BglG and LicT. Here, we demonstrate that the activity of LevR is regulated by two phosphoenolpyruvate (PEP)-dependent phosphorylation reactions catalysed by the phosphotransferase system (PTS), a transport system for sugars, polyols and other sugar derivatives. The two general components of the PTS, enzyme I and HPr, and the two soluble, sugar-specific proteins of the lev-PTS, LevD and LevE, form a signal transduction chain allowing the PEP-dependent phosphorylation of LevR, presumably at His-869. This phosphorylation seems to inhibit LevR activity and probably regulates the induction of the lev operon. Mutants in which His-869 of LevR has been replaced with a non-phosphorylatable alanine residue exhibited constitutive expression from the lev promoter, as do levD or levE mutants. In contrast, PEP-dependent phosphorylation of LevR in the presence of only the general components of the PTS, enzyme I and HPr, regulates LevR activity positively. This phosphorylation most probably occurs at His-585. Mutants in which His-585 has been replaced with an alanine had lost stimulation of LevR activity and PEP-dependent phosphorylation by enzyme I and HPr. This second phosphorylation of LevR at His-585 is presumed to play a role in carbon catabolite repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00781.x
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  • 12
    Electronic Resource
    Electronic Resource
    Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 31 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The transcriptional antiterminator LicT regulates the induction and carbon catabolite repression of the Bacillus subtilis bglPH operon. LicT is inactive in mutants affected in one of the two general components of the phosphoenolpyruvate (PEP):glycose phosphotransferase system, enzyme I or histidine-containing protein (HPr). We demonstrate that LicT becomes phosphorylated in the presence of PEP, enzyme I and HPr. The phosphoryl group transfer between HPr and LicT is reversible. Phosphorylation of LicT with PEP, enzyme I and HPr led to the appearance of three additional LicT bands on polyacrylamide–urea gels. These bands probably correspond to one-, two- and threefold phosphorylated LicT. After phosphorylation of LicT with [32P]-PEP, enzyme I and HPr, proteolytic digestion of [32P]-P-LicT, separation of the peptides by reverse-phase chromatography, mass spectrometry and N-terminal sequencing of radiolabelled peptides, three histidyl residues were found to be phosphorylated in LicT. These three histidyl residues (His-159, His-207 and His-269) are conserved in most members of the BglG/SacY family of transcriptional antiterminators. Phosphorylation of LicT in the presence of seryl-phosphorylated HPr (P-Ser-HPr) was much slower compared with its phosphorylation in the presence of HPr. The slower phosphorylation in the presence of P-Ser-HPr leading to reduced LicT activity is presumed to play a role in a recently described LicT-mediated CcpA-independent carbon catabolite repression mechanism operative for the bglPH operon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01262.x
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  • 13
    Electronic Resource
    Electronic Resource
    Elaborate transcription regulation of the Bacillus subtilis ilv-leu operon involved in the biosynthesis of branched-chain amino acids through global regulators of CcpA, CodY and TnrA (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 56 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Bacillus subtilis ilv-leu operon involved in the biosynthesis of branched-chain amino acids is under negative regulation mediated by TnrA and CodY, which recognize and bind to their respective cis-elements located upstream of the ilv-leu promoter. This operon is known to be under CcpA-dependent positive regulation. We have currently identified a catabolite-responsive element (cre) for this positive regulation (bases −96 to −82; +1 is the ilv-leu transcription initiation base) by means of DNase I-footprinting in vitro, and deletion and base-substitution analyses of cre. Under nitrogen-rich growth conditions in glucose-minimal medium supplemented with glutamine and amino acids, CcpA and CodY exerted positive and negative regulation of ilv-leu, respectively, but TnrA did not function. Moreover, CcpA and CodY were able to function without their counteracting regulation of each other, although the CcpA-dependent positive regulation did not overcome the CodY-dependent negative regulation. Furthermore, under nitrogen-limited conditions in glucose-minimal medium with glutamate as the sole nitrogen source, CcpA and TnrA exerted positive and negative regulation, respectively, but CodY did not function. This CcpA-dependent positive regulation occurred without the TnrA-dependent negative regulation. However, the TnrA-dependent negative regulation did not occur without the CcpA-dependent positive regulation, raising the possibility that this negative regulation might decrease the CcpA-dependent positive regulation. The physiological role of this elaborate transcription regulation of the B. subtilis ilv-leu operon in overall metabolic regulation in this organism is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04635.x
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  • 14
    Electronic Resource
    Electronic Resource
    Analysis of a ptsH homologue from Streptomyces coelicolor A3(2) (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 177 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A ptsH homologue of Streptomyces coelicolor A3(2) was identified in the emerging genome sequence, cloned in Escherichia coli and the S. coelicolor HPr over-produced and purified. The protein was phosphorylated in vitro in a phosphoenolpyruvate (PEP)-dependent manner by purified enzyme I (EI) from Bacillus subtilis, and much less efficiently in an ATP-dependent manner by purified HPr kinase, also from B. subtilis. There was no indication of ATP-dependent phosphorylation of the purified protein by cell extracts of either S. coelicolor or Streptomyces lividans. Deletion of the ptsH homologue from the S. coelicolor and S. lividans chromosomes had no effect on growth when fructose was supplied as sole carbon source, and in S. coelicolor it had no effect on glucose repression of agarase and galactokinase synthesis, suggesting that the HPr encoded by this gene does not play an essential role in fructose transport nor a general role in carbon catabolite repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13744.x
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  • 15
    Electronic Resource
    Electronic Resource
    Phosphoenolpyruvate-dependent phosphorylation of a 55-kDa protein of Streptococcus faecalis catalyzed by the phosphotransferase system (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 29 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A protein with an Mr of 55000 was isolated from glucose-grown Streptococcus faecalis cells. The protein becomes phosphorylated in a phosphoenolpyruvate-dependent reaction catalyzed by enzyme I and HPr of the bacterial phosphotransferase system. It did not stimulate phosphoenolpyruvate-dependent glucose phosphorylation. Several sugars were tested for their ability to dephosphorylate the phosphorylated protein in the presence of membrane fragments. Even though some of the sugars were able to dephosphorylate phospho-HPr quickly, the factor III-like 55-kDa protein remained phosphorylated. We therefore assumed that this protein is not involved in any sugar uptake reaction but that it exerts a regulatory function in Gram-positive bacteria comparable to the function of factor III specific for glucose in Escherichia coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00869.x
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  • 16
    Electronic Resource
    Electronic Resource
    Gemeinsame Kontrolle von Zellwachstum und Transportfunktionen in einer Nierenzellinie (1988)
    Springer
    Naturwissenschaften 75 (1988), S. 451-457 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00364025
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  • 17
    Electronic Resource
    Electronic Resource
    The role of phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, in the regulation of carbon metabolism in gram-positive bacteria (1993)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 51 (1993), S. 19-24 
    Details
    ISSN: 0730-2312
    Keywords: phosphotransferase system ; HPr ; sugar transport ; gram-positive bacteria ; protein kinase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: HPr of the Gram-positive bacterial phosphotransferase system (PTS) can be phosphorylated by an ATP-dependent protein kinase on a serine residue or by PEP-dependent Enzyme I on a histidyl residue. Both phosphorylation events appear to influence the metabolism of non-PTS carbon sources. Catabolite repression of the gluconate (gnt) operon of B. subtilis appears to be regulated by the former phosphorylation event, while glycerol kinase appears to be regulated by the latter phosphorylation reaction. The extent of our understanding of these processes will be described. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240510105
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  • 18
    Electronic Resource
    Electronic Resource
    Darstellung und Molekülstruktur eines Metallclusters mit Cubanstruktur, [η5-C5H5Mo(CO)3HgMo] 4 (1979)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 112 (1979), S. 2413-2418 
    Details
    ISSN: 0009-2940
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Synthesis and Molecular Structure of a Metal Cluster with Cubane Structure, [η5-C5H5Mo(CO)3HgMo]4(4)The compound [η5-C5H5Mo(CO)3HgMo]4 has been isolated as an additional product of the reaction between [η5-C5H5Mo(CO)3]2, 2-butenyl chloride, and sodium amalgam. The X-ray structure (R = 0·050) analysis of this novel species revealed that the compound has a slightly distorted cubane structure, for the first time the cubane unit being built up by two different metal atoms (Mo and Hg).
    Notes: Die Verbindung [η5-C5H5Mo(CO)3HgMo]4 (4) wurde als weiteres Produkt der Reaktion zwischen [η5-C5H5Mo(CO)3]2, 2-Butenylchlorid und Natriumamalgam isoliert. Die Röntgenstrukturanalyse dieser neuartigen Spezies zeigt eine leicht verzerrte Cubanstruktur, bei der das Cubangerüst erstmals aus zwei verschiedenen Metallatomen (Mo und Hg) aufgebaut ist. Der R-Wert beträgt 0·050.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cber.19791120708
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  • 19
    Electronic Resource
    Electronic Resource
    Die Rolle des bakteriellen Phosphotransferase-Systems im Zuckermetabolismus (1988)
    Weinheim : Wiley-Blackwell
    Biologie in unserer Zeit 18 (1988), S. 9-15 
    Details
    ISSN: 0045-205X
    Keywords: Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/biuz.19880180103
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  • 20
    Electronic Resource
    Electronic Resource
    Proteinphosphorylierung in Bakterien - Regulation von Genexpression, Transportfunktionen und Stoffwechselvorgängen (1988)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 100 (1988), S. 1072-1082 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die wichtige Rolle der Proteinphosphorylierung zur Regulation der unterschiedlichsten Prozesse in eukaryontischen Zellen ist seit langem bekannt und sehr gut untersucht; der eindeutige Nachweis der Proteinphosphorylierung in Bakterien gelang dagegen erst vor weniger als einem Jahrzehnt. Mittlerweile kennt man fünf bakterielle Proteine, deren Aktivität durch reversible Phosphorylierung kontrolliert wird: Die Phosphorylierung der Isocitrat-Dehydrogenase steuert unter bestimmten Wachstumsbedingungen den weiteren Abbauweg von Isocitrat über entweder den Citratcyclus oder den Glyoxylatcyclus. Die Phosphorylierung von HPr, einem Phosphorylcarrier-Protein des Phosphotransferase-Systems, reguliert in Gram-positiven Bakterien die Kohlenhydrataufnahme über dieses Transportsystem. Die Phosphorylierung der Glycerin-Kinase in Streptococcus faecalis reguliert den Transport und den Abbau von Glycerin. Die Phosphorylierung des Stickstoffregulator-Proteins I (NRI) in E. coli steuert die Genexpression der Enzyme, die am Stickstoffmetabolismus beteiligt sind. Die Phosphorylierung der Citrat-Lyase-Ligase bei Clostridium sphenoides schließlich reguliert die Umwandlung der Citrat-Lyase von der inaktiven Mercapto- in die aktive Acetylform und damit den weiteren Abbauweg von Citrat. Neuere Untersuchungen haben gezeigt, daß in E. coli mehr als hundert Proteine phosphoryliert werden. Man darf daher erwarten, daß die Proteinphosphorylierung bei Bakterien eine genauso wichtige Rolle bei der Regulation der zellulären Prozesse spielt, wie dies bei Eukaryontenzellen der Fall ist.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19881000807
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