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  • 1
    Electronic Resource
    Electronic Resource
    Structure of Major Surface Determinants and DNA Diagnosis of Pneumocystis carinii (1989)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 36 (1989), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Pneumocystis carinii is a pathogen which, causes fatal pneumonia in patients with the acquired immune deficiency syndrome (AIDS). To facilitate the basic study of P. carinii, we have analyzed its major surface proteins by both immunochemical and biochemical methods. The major protein components of both cysts and trophozoites are a group of proteins called “P115” with apparent masses of 105–120 kd. It includes 6 isoelcclric variants. A monoclonal antibody raised against cysts recognizes all 6 variants and reacts with epitopes located in the cell wall indicating that P115 is an immunorcactive surface component. The isoelectric variants contain identical or closely related protein components and they are mannose-rich glycoproteins. The isoelectric variation may be due primarily to differences in glycosylation. The majority of sera from humans with diagnosed pneumocystosis that were tested reacted strongly with the P115 proteins. To develop probes for DNA diagnosis and to facilitate molecular studies, a genomic DNA library of P. carinii has been constructed. Some of these clones were used for DNA hybridization analysis of rat and human lungs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1989.tb02699.x
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  • 2
    Electronic Resource
    Electronic Resource
    5S Ribosomal RNA Sequence of Pneumocystis carinii and its Phylogenetic Association with “Rhizopoda/Myxomycota/Zygomycota Group” (1989)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 36 (1989), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cytoplasmic 5S ribosomal RNA sequence from Pneumocystis carinii was determined and compared with those of 382 eukaryotes and an evolutionary tree was constructed to establish the phylogenetic position of Pneumocystis. The data suggest that Pneumocystis is associated with the Rhizopoda/Myxomycota/ Zygomycota group but not with common fungi, such as Ascomycota or Basidiomycota, nor with other protozoa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1989.tb05812.x
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  • 3
    Electronic Resource
    Electronic Resource
    5S Ribosomal RNA Sequence of Pneumocystis carinii and its Phylogenetic Association with “Rhizopoda/Myxomycota/Zygomycota Group” (1989)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 36 (1989), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cytoplasmic 58 ribosomal RNA sequence from Pneumocystis carinii was determined and compared with those of 382 eukaryotes and an evolutionary tree was constructed to establish the phylogenetic position of Pneumocystis. The data suggest that Pneumocystis is associated with the RhizopodaAlyxomycota/ Zygomycota group but not with common fungi, such as Ascomycota or Basidiomycoia, nor with other protozoa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1989.tb02671.x
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  • 4
    Electronic Resource
    Electronic Resource
    Antigenic Variation by Telomeric Recombination of Major-Surface-Glycoprotein Genes of Pneumocystis carinii (1996)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 43 (1996), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1996.tb04949.x
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  • 5
    Electronic Resource
    Electronic Resource
    Structure of Major Surface Determinants and DNA Diagnosis of Pneumocystis carinii (1989)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 36 (1989), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Pneumocystis carinii is a pathogen which causes fatal pneumonia in patients with the acquired immune deficiency syndrome (AIDS). To facilitate the basic study of P. carinii, wc have analyzed its major surface proteins by both immunochemical and biochemical methods. The major protein components of both cysts and trophozoites are a group of proteins called “PI 15” with apparent masses of 105–120 kd. It includes 6 isoelectric variants. A monoclonal antibody raised against cysts recognizes all 6 variants and reacts with epitopes located in the cell wall indicating that PI 15 is an immunoreactive surface component. The isoelectric variants contain identical or closely related protein components and they are mannose-rich glycoproteins. The isoelectric variation may be due primarily to differences in glycosylation. The majority of sera from humans with diagnosed pneumocystosis that were tested reacted strongly with the PI 15 proteins. To develop probes for DNA diagnosis and to facilitate molecular studies, a genomic DNA library of P. carinii has been constructed. Some of these clones were used for DNA hybridization analysis of rat and human lungs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1989.tb05832.x
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  • 6
    Electronic Resource
    Electronic Resource
    Pleiotropic effects of the rpoC10 mutation affecting the RNA polymerase β′ subunit of Escherichia coli on factor-dependent transcription termination and antitermination (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 9 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Escherichia coli RNA polymerase is composed of four different subunits, 2α, β, β′ and σ;. Among these subunits, the role of β′ is poorly understood. The rpoC10 mutation affecting β′ has been isolated as a suppressor mutation of the temperature-sensitive nusA11 mutant. DNA sequence analysis revealed that the rpoC10 mutant is a substitution of Lys for Glu-402. This increased positive charge appears to compensate for the increased negative charge present in the nusA11 protein (Asp for Gly-181). In vivo measurements of reporter gene expression have revealed that rpoC10 restores ρ-dependent termination but fails to restore ρ-independent termination in nusA.11 Moreover, the rpoC10 mutation, in combination with any nusA mutation, inhibited λ Q-mediated antitermination without affecting N antitermination and severely restricted λ phage development. The inhibition of Q function and λ growth could be compensated for by overproducing Q. These results suggest that the RNA polymerase β′ subunit plays a crucial rote in factor-dependent transcription termination and antitermination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01690.x
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  • 7
    Electronic Resource
    Electronic Resource
    A transcription terminator signal necessary for plasmid Collb-P9 replication (1995)
    Osney Mead, Oxford OX2 0EL, UK : Blackwell Scientific Publications
    Molecular microbiology 17 (1995), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Replication of the Inclα plasmid CoIIb-P9 requires the repZ gene, which encodes an essential, unstable initiator protein termed RepZ. Although many functional features of the CoIIb-P9 replicon resemble those of structurally unrelated IncFII plasmids R1 and NR1, the role of transcription of repZ towards the replication origin is poorly understood. Using a series of deletion and substitution mutants of the CoIIb-P9 replicon, we found that RepZ prefers to act in cis and that a spacer sequence between repZ and the origin is required for replication. This spacer element, referred to as CIS, retained strong transcription terminator activity. Efficient transcription terminators, whether Rho-dependent or -independent, were capable of replacing CIS function for in vivo replication; CoIIb-P9 replicated better as transcription terminated more efficiently within CIS. When the CIS element was substituted for by a strong Rho-dependent terminator, such as λ tR1 or E. coli trp tt', in vivo replication of these recombinant replicons became dependent on the Rho factor, in contrast to the authentic CoIIb-P9 replicon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1995.mmi_17020291.x
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  • 8
    Electronic Resource
    Electronic Resource
    Control and function of lysyl-tRNA synthetases: diversity and co-ordination (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: Lysyl-tRNA synthetases are synthesized from two distinct genes in Escherichia coli, lysS (constitutively) and lysU (inducibly); however, the physiological significance and the differential control mechanism of these two genes have been a long-standing puzzle. Recent studies have successfully uncovered a significant control mechanism of lysU expression, which involves the leucine-responsive regulatory protein (Lrp) and a translational enhancer element called‘downstream box'. Moreover, it is likely that there is a mechanism underlying co-ordinate expression of lysU with other genes outside the leucine-Lrp regulon under harsh conditions such as low pH and anaerobiosis. A possible mechanism of lysyl-tRNA synthetase expression and function is reviewed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01948.x
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  • 9
    Electronic Resource
    Electronic Resource
    Heterologous expression of Aquifex aeolicus ribosome recycling factor in Escherichia coli is dominant lethal by forming a complex that lacks functional co-ordination for ribosome disassembly (2005)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Recycling the post-termination ribosomal complex requires the co-ordinated effort of the ribosome, ribosome  recycling  factor  (RRF)  and  elongation  factor EF-G. Although Aquifex aeolicus RRF (aaRRF) binds Escherichia coli ribosomes as efficiently as E. coli RRF, the resulting complex is non-functional and dominant lethal in E. coli, even in the presence of homologous A. aeolicus EF-G. These findings suggest that the E. coli post-termination ribosomal complex with aaRRF lacks functional co-ordination with EF-G required for ribosome recycling. A chimeric EF-G (E. coli domains I–III, A. aeolicus domains IV–V) or an A. aeolicus EF-G with distinct mutations in the domain I–II interface could activate aaRRF. Furthermore, novel mutations that localize to one surface of the  L-shape  structure  of  aaRRF  restored  activity  in E. coli. These aaRRF mutations are spatially distinct from mutations previously described and suggest a novel active centre for coupling EF-G's G domain motor action to ribosome disassembly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04387.x
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  • 10
    Electronic Resource
    Electronic Resource
    Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor G (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Ribosome recycling factor (RRF) disassembles post-termination ribosomal complexes in concert with elongation factor EF-G freeing the ribosome for a new round of polypeptide synthesis. How RRF interacts with EF-G and disassembles post-termination ribosomes is unknown. RRF is structurally similar to tRNA and is therefore thought to bind to the ribosomal A site and be translocated by EF-G during ribosome disassembly as a mimic of tRNA. However, EF-G variants that remain active in GTP hydrolysis but are defective in tRNA translocation fully activate RRF function in vivo and in vitro. Furthermore, RRF and the GTP form of EF-G do not co-occupy the terminating ribosome in vitro; RRF is ejected by EF-G from the preformed complex. These findings suggest that RRF is not a functional mimic of tRNA and disassembles the post-termination ribosomal complex independently of the translocation activity of EF-G.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04156.x
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