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  • 1
    Electronic Resource
    Electronic Resource
    BIOGENESIS, ARCHITECTURE, AND FUNCTION OF BACTERIAL TYPE IV SECRETION SYSTEMS (2005)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 59 (2005), S. 451-485 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Type IV secretion (T4S) systems are ancestrally related to bacterial conjugation machines. These systems assemble as a translocation channel, and often also as a surface filament or protein adhesin, at the envelopes of Gram-negative and Gram-positive bacteria. These organelles mediate the transfer of DNA and protein substrates to phylogenetically diverse prokaryotic and eukaryotic target cells. Many basic features of T4S are known, including structures of machine subunits, steps of machine assembly, substrates and substrate recognition mechanisms, and cellular consequences of substrate translocation. A recent advancement also has enabled definition of the translocation route for a DNA substrate through a T4S system of a Gram-negative bacterium. This review emphasizes the dynamics of assembly and function of model conjugation systems and the Agrobacterium tumefaciens VirB/D4 T4S system. We also summarize salient features of the increasingly studied effector translocator systems of mammalian pathogens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.micro.58.030603.123630
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  • 2
    Electronic Resource
    Electronic Resource
    Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines (2001)
    Oxford, UK : Blackwell Science, Ltd
    Molecular microbiology 40 (2001), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Bacterial conjugation systems are highly promiscuous macromolecular transfer systems that impact human health significantly. In clinical settings, conjugation is exceptionally problematic, leading to the rapid dissemination of antibiotic resistance genes and other virulence traits among bacterial populations. Recent work has shown that several pathogens of plants and mammals –Agrobacterium tumefaciens, Bordetella pertussis, Helicobacter pylori and Legionella pneumophila– have evolved secretion pathways ancestrally related to conjugation systems for the purpose of delivering effector molecules to eukaryotic target cells. Each of these systems exports distinct DNA or protein substrates to effect a myriad of changes in host cell physiology during infection. Collectively, secretion pathways ancestrally related to bacterial conjugation systems are now referred to as the type IV secretion family. The list of putative type IV family members is increasing rapidly, suggesting that macromolecular transfer by these systems is a widespread phenomenon in nature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02302.x
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  • 3
    Electronic Resource
    Electronic Resource
    Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 32 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The Agrobacterium tumefaciens VirB4 ATPase functions with other VirB proteins to export T-DNA to susceptible plant cells and other DNA substrates to a variety of prokaryotic and eukaryotic cells. Previous studies have demonstrated that VirB4 mutants with defects in the Walker A nucleotide-binding motif are non-functional and exert a dominant negative phenotype when synthesized in wild-type cells. This study characterized the oligomeric structure of VirB4 and examined the effects of Walker A sequence mutations on complex formation and transporter activity. VirB4 directed dimer formation when fused to the amino-terminal portion of cI repressor protein, as shown by immunity of Escherichia coli cells to λ phage infection. VirB4 also dimerized in Agrobacterium tumefaciens, as demonstrated by the recovery of a detergent-resistant complex of native protein and a functional, histidine-tagged derivative by precipitation with anti-His6 antibodies and by Co2+ affinity chromatography. Walker A sequence mutants directed repressor dimerization in E. coli and interacted with His-VirB4 in A. tumefaciens, indicating that ATP binding is not required for self-association. A dimerization domain was localized to a proposed N-terminal membrane-spanning region of VirB4, as shown by the dominance of an allele coding for the N-terminal 312 residues and phage immunity of host cells expressing cI repressor fusions to alleles for the first 237 or 312 residues. A recent study reported that the synthesis of a subset of VirB proteins, including VirB4, in agrobacterial recipients has a pronounced stimulatory effect on the virB-dependent conjugal transfer of plasmid RSF1010 by agrobacterial donors. VirB4′312 suppressed the stimulatory effect of VirB proteins for DNA uptake when synthesized in recipient cells. In striking contrast, Walker A sequence mutants contributed to the stimulatory effect of VirB proteins to the same extent as native VirB4. These findings indicate that the oligomeric structure of VirB4, but not its capacity to bind ATP, is important for the assembly of VirB proteins as a DNA uptake system. The results of these studies support a model in which VirB4 dimers or homomultimers contribute structural information for the assembly of a transenvelope channel competent for bidirectional DNA transfer, whereas an ATP-dependent activity is required for configuring this channel as a dedicated export machine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01436.x
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  • 4
    Electronic Resource
    Electronic Resource
    VirE2, a Type IV secretion substrate, interacts with the VirD4 transfer protein at cell poles of Agrobacterium tumefaciens (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 49 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Agrobacterium tumefaciens transfers oncogenic DNA and effector proteins to plant cells during the course of infection. Substrate translocation across the bacterial cell envelope is mediated by a type IV secretion (TFS) system composed of the VirB proteins, as well as VirD4, a member of a large family of inner membrane proteins implicated in the coupling of DNA transfer intermediates to the secretion machine. In this study, we demonstrate with novel cytological screens – a two-hybrid (C2H) assay and bimolecular fluorescence complementation (BiFC) – and by immunoprecipitation of chemically cross-linked protein complexes that the VirE2 effector protein interacts directly with the VirD4 coupling protein at cell poles of A. tumefaciens. Analyses of truncation derivatives showed that VirE2 interacts via its C terminus with VirD4, and, further, an NH2-terminal membrane-spanning domain of VirD4 is dispensable for complex formation. VirE2 interacts with VirD4 independently of the virB-encoded transfer machine and T pilus, the putative periplasmic chaperones AcvB and VirJ, and the T-DNA transfer intermediate. Finally, VirE2 is recruited to polar-localized VirD4 as a complex with its stabilizing secretion chaperone VirE1, yet the effector–coupling protein interaction is not dependent on chaperone binding. Together, our findings establish for the first time that a protein substrate of a type IV secretion system is recruited to a member of the coupling protein superfamily.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03669.x
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  • 5
    Electronic Resource
    Electronic Resource
    Agrobacterium tumefaciens oncogenic suppressors inhibit T-DNA and VirE2 protein substrate binding to the VirD4 coupling protein (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 58 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Agrobacterium tumefaciens uses a type IV secretion (T4S) system composed of VirB proteins and VirD4 to deliver oncogenic DNA (T-DNA) and protein substrates to susceptible plant cells during the course of infection. Here, by use of the Transfer DNA ImmunoPrecipitation (TrIP) assay, we present evidence that the mobilizable plasmid RSF1010 (IncQ) follows the same translocation pathway through the VirB/D4 secretion channel as described previously for the T-DNA. The RSF1010 transfer intermediate and the Osa protein of plasmid pSa (IncW), related in sequence to the FiwA fertility inhibition factor of plasmid RP1 (IncPα), render A. tumefaciens host cells nearly avirulent. By use of a semi-quantitative TrIP assay, we show that both of these ‘oncogenic suppressor factors’ inhibit binding of T-DNA to the VirD4 substrate receptor. Both factors also inhibit binding of the VirE2 protein substrate to VirD4, as shown by coimmunoprecipitation and bimolecular fluorescence complementation assays. Osa fused to the green fluorescent protein (GFP) also blocks T-DNA and VirE2 binding to VirD4, and Osa-GFP colocalizes with VirD4 at A. tumefaciens cell poles. RSF1010 and Osa interfere specifically with VirD4 receptor function and not with VirB channel activity, as shown by (i) TrIP and (ii) a genetic screen for effects of the oncogenic suppressors on pCloDF13 translocation through a chimeric secretion channel composed of the pCloDF13-encoded MobB receptor and VirB channel subunits. Our findings establish that a competing plasmid substrate and a plasmid fertility inhibition factor act on a common target, the T4S receptor, to inhibit docking of DNA and protein substrates to the translocation apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04852.x
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  • 6
    Electronic Resource
    Electronic Resource
    Energetic components VirD4, VirB11 and VirB4 mediate early DNA transfer reactions required for bacterial type IV secretion (2004)
    Oxford, UK : Blackwell Publishing Ltd.
    Molecular microbiology 54 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Bacteria use type IV secretion systems (T4SS) to translocate DNA (T-DNA) and protein substrates across the cell envelope. By transfer DNA immunoprecipitation (TrIP), we recently showed that T-DNA translocates through the Agrobacterium tumefaciens VirB/D4 T4SS by forming close contacts sequentially with the VirD4 receptor, VirB11 ATPase, the inner membrane subunits VirB6 and VirB8 and, finally, VirB2 pilin and VirB9. Here, by TrIP, we show that nucleoside triphosphate binding site (Walker A motif) mutations do not disrupt VirD4 substrate binding or transfer to VirB11, suggesting that these early reactions proceed independently of ATP binding or hydrolysis. In contrast, VirD4, VirB11 and VirB4 Walker A mutations each arrest substrate transfer to VirB6 and VirB8, suggesting that these subunits energize this transfer reaction by an ATP-dependent mechanism. By co-immunoprecipitation, we supply evidence for VirD4 interactions with VirB4 and VirB11 independently of other T4SS subunits or intact Walker A motifs, and with the bitopic inner membrane subunit VirB10. We reconstituted substrate transfer from VirD4 to VirB11 and to VirB6 and VirB8 by co-synthesis of previously identified ‘core’ components of the VirB/D4 T4SS. Our findings define genetic requirements for DNA substrate binding and the early transfer reactions of a bacterial type IV translocation pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04345.x
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  • 7
    Electronic Resource
    Electronic Resource
    Impact of low-temperature stress on general phenylpropanoid and anthocyanin pathways: Enhancement of transcript abundance and anthocyanin pigmentation in maize seedlings (1994)
    Springer
    Planta 194 (1994), S. 541-549 
    Details
    ISSN: 1432-2048
    Keywords: Anthocyanin ; Cold stress ; mRNA ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Changes in anthocyanin content and transcript abundance for genes whose products function in general phenylpropanoid metabolism and the anthocyanin pathway were monitored in maize (Zea mays L.) seedlings during short-term, low-temperature treatment. Anthocyanin and mRNA abundance in sheaths of maize seedlings increased with the severity and duration of cold. Anthocyanin accumulation was found in all tested lines that were genotypically capable of any anthocyanin production. Within 24 h of transferring 7-d maize (B37N) seedlings to 10° C, phenylalanine ammonia-lyase (Pal) (EC 4.3.1.5)-homologous and chalcone synthase (C2) (EC 2.3.1.74) transcript levels increased at least 8- and 50-fold, respectively, and 4-coumarate:CoA ligase (4Cl) (EC 6.2.1.12)-homologous and chalcone isomerase (Chi) (EC 5.5.1.6)-homologous transcripts increased at least 3-fold over levels in unstressed plants. Time-course studies showed thatPal (EC 4.3.1.5) andC2-transcript levels remained relatively constant for the first 12 h of cold stress, dramatically increased over the next 12 h, and declined to pretreatment levels within 2 d of returning coldstressed seedlings to ambient (25° C) temperature. Transcripts4Cl (EC 6.2.1.12) andChi (EC 5.5.1.6) increased in abundance within 6 h of cold stress, exhibited no further increase over the next 36 h, and declined to pretreatment levels upon returning seedlings to 25° C. Transcripts homologous to two regulatory (R, C1) and three structural (A1,A2, andBz2) anthocyanin genes increased at least 7- to 10-fold during cold treatment, exhibiting similar kinetics of accumulation as forPal (EC 4.3.1.5) andC2 transcripts. Transcripts encoded byBz1, the anthocyanin structural gene for UDP:glucose-flavonol glucosyltransferase (EC 2.4.1.91), were relatively abundant in control tissues and exhibited only a transient increase during the cold period. Our studies suggest that the genes of the anthocyanin biosynthetic pathway can be consideredcor (Cold-Regulation) genes, and because this pathway is well defined, it is an excellent subject for characterizing plant molecular responses to low temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00714468
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  • 8
    Electronic Resource
    Electronic Resource
    Interspecific complementary and competitive interactions between intercropped maize and faba bean (1999)
    Springer
    Plant and soil 212 (1999), S. 105-114 
    Details
    ISSN: 1573-5036
    Keywords: intercropping ; interspecific facilitation ; land equivalent ratio ; relative crowding coefficient ; root interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Interspecific complementary and competitive interactions between maize (Zea mays L. cv. Zhongdan No. 2) and faba bean (Vicia faba L. cv. Linxia Dacaidou) in maize/faba bean intercropping systems were assessed in two field experiments in Gansu province, northwestern China, plus a microplot experiment in one treatment of one of the field experiments in which root system partitions were used to determine interspecific root interactions. Intercropping effects were detected, with land equivalent ratio values of 1.21–1.23 based on total (grain+straw) yield and 1.13–1.34 based on grain yield. When two rows of maize were intercropped with two rows of faba bean, both total yield and grain yield of both crop species were significantly higher than those of sole maize and faba bean on an equivalent area basis. When two rows of pea (Pisum sativum L. cv. Beijing No. 5) were intercropped with two rows of faba bean, neither total yield nor grain yield of faba bean was higher than of sole faba bean on an equivalent area basis. Interspecific competition between maize and faba bean was relatively weak, with mean relative crowding coefficients of 0.99–1.02 for maize and 1.55–1.59 for faba bean. The microplot experiment in which partitions were placed between root systems showed a significant positive yield effect on maize when the root systems intermingled freely (no partition) or partly (400 mesh nylon net partition) compared with no interspecific root interaction (plastic sheet partition).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004656205144
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  • 9
    Electronic Resource
    Electronic Resource
    Polytetrazoles and polyaminotetrazoles (1968)
    New York : Wiley-Blackwell
    Journal of Polymer Science Part A-1: Polymer Chemistry 6 (1968), S. 729-742 
    Details
    ISSN: 0449-296X
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Polyaminotetrazoles were obtained by the action of hydrazoic acid on solutions of polycarbodimides prepared from methylenebis(4-phenyl isocyanate), toluene 2,4-diisocyanate, 3,3′-dimethoxy-4,4′-biphenylene diisocyanate, mesitylene diisocyanate, and hexamethylene diisocyanate. The polyaminotetrazoles, which were soluble only in concentrated sulfuric acid, had inherent viscosities of 0.12-0.78. Polymerization of the disodium salts of bistetrazoles with α,ω-dihalides gave polytetrazoles without the secondary amine linkage in the chain. The bistetrazoles, used were methylenebis(5-tetrazole) and 5,5′-p-phenylenebistetrazole, and the dihalides were α,α′-dichloro-p-xylene, 1,2-dibromoethane, and 1,4-dibromobutane. The polytetrazoles were soluble in concentrated sulfuric acid and had low inherent viscosities, 0.08-0.17. Thermogravimetric analyses showed that marked degradation of both classes of polymers occured at 250-300°C.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1968.150060402
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  • 10
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    High nitrogen deposition in an agricultural ecosystem of Shaanxi, China (2016)
    Springer
    Details
    Publication Date: 2016-03-29
    Print ISSN: 0944-1344
    Electronic ISSN: 1614-7499
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Published by Springer
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