Relevant bibliographies by topics / Bacterial complementation

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Academic literature on the topic 'Bacterial complementation'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Bacterial complementation"

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Fröderberg, Linda, Thomas Röhl, Klaas-Jan van Wijk, and Jan-Willem L. de Gier. "Complementation of bacterial SecE by a chloroplastic homologue." FEBS Letters 498, no. 1 (May 30, 2001): 52–56. http://dx.doi.org/10.1016/s0014-5793(01)02494-2.

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Crépin, Sébastien, Josée Harel, and Charles M. Dozois. "Chromosomal Complementation Using Tn7Transposon Vectors in Enterobacteriaceae." Applied and Environmental Microbiology 78, no. 17 (June 15, 2012): 6001–8. http://dx.doi.org/10.1128/aem.00986-12.

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ABSTRACTGenetic complementation in many bacteria is commonly achieved by reintroducing functional copies of the mutated or deleted genes on a recombinant plasmid. Chromosomal integration systems using the Tn7transposon have the advantage of providing a stable single-copy integration that does not require selective pressure. Previous Tn7systems have been developed, although none have been shown to work effectively in a variety of enterobacteria. We have developed several mini-Tn7and transposase vectors to provide a more versatile system. Transposition of Tn7at the chromosomalattTn7site was achieved by a classical conjugation approach, wherein the donor strain harbored the mini-Tn7vector and the recipient strain possessed the transposase vector. This approach was efficient for five different pathogenic enterobacterial species. Thus, this system provides a useful tool for single-copy complementation at an episomal site for research in bacterial genetics and microbial pathogenesis. Furthermore, these vectors could also be used for the introduction of foreign genes for use in biotechnology applications, vaccine development, or gene expression and gene fusion constructs.
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Merkel, Susan, Adam Parks, and Buck Hanson. "A Small Group Activity About Bacterial Regulation And Complementation †." Journal of Microbiology & Biology Education 11, no. 2 (December 20, 2010): 152–55. http://dx.doi.org/10.1128/jmbe.v11i2.196.

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Cahoon, Laty A., and Nancy E. Freitag. "Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone." Infection and Immunity 83, no. 10 (July 27, 2015): 4028–41. http://dx.doi.org/10.1128/iai.00504-15.

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The Gram-positive bacteriumListeria monocytogenesis a facultative intracellular pathogen that relies on the regulated secretion and activity of a variety of proteins that sustain life within diverse environments. PrsA2 has recently been identified as a secreted peptidyl-prolylcis/transisomerase and chaperone that is dispensable for bacterial growth in broth culture but essential forL. monocytogenesvirulence. Following host infection, PrsA2 contributes to the proper folding and activity of secreted proteins that are required for bacterial replication within the host cytosol and for bacterial spread to adjacent cells. PrsA2 is one member of a family of Gram-positive secretion chaperones that appear to play important roles in bacterial physiology; however, it is not known how these proteins recognize their substrate proteins or the degree to which their function is conserved across diverse Gram-positive species. We therefore examined PrsA proteins encoded by a variety of Gram-positive bacteria for functional complementation ofL. monocytogenesmutants lackingprsA2. PrsA homologues encoded byBacillus subtilis,Streptococcus pyogenes,Streptococcus pneumoniae,Streptococcus mutans,Staphylococcus aureus, andLactococcus lactiswere examined for functional complementation of a variety ofL. monocytogenesPrsA2-associated phenotypes central toL. monocytogenespathogenesis and bacterial cell physiology. Our results indicate that while selected aspects of PrsA2 function are broadly conserved among diverse Gram-positive bacteria, PrsA2 exhibits unique specificity forL. monocytogenestarget proteins required for pathogenesis. TheL. monocytogenesPrsA2 chaperone thus appears evolutionarily optimized for virulence factor secretion within the host cell cytosol while still maintaining aspects of activity relevant to more general features of Gram-positive protein translocation.
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Pribat, Anne, Linda Jeanguenin, Aurora Lara-Núñez, Michael J. Ziemak, John E. Hyde, Valérie de Crécy-Lagard, and Andrew D. Hanson. "6-Pyruvoyltetrahydropterin Synthase Paralogs Replace the Folate Synthesis Enzyme Dihydroneopterin Aldolase in Diverse Bacteria." Journal of Bacteriology 191, no. 13 (April 24, 2009): 4158–65. http://dx.doi.org/10.1128/jb.00416-09.

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ABSTRACT Dihydroneopterin aldolase (FolB) catalyzes conversion of dihydroneopterin to 6-hydroxymethyldihydropterin (HMDHP) in the classical folate biosynthesis pathway. However, folB genes are missing from the genomes of certain bacteria from the phyla Chloroflexi, Acidobacteria, Firmicutes, Planctomycetes, and Spirochaetes. Almost all of these folB-deficient genomes contain an unusual paralog of the tetrahydrobiopterin synthesis enzyme 6-pyruvoyltetrahydropterin synthase (PTPS) in which a glutamate residue replaces or accompanies the catalytic cysteine. A similar PTPS paralog from the malaria parasite Plasmodium falciparum is known to form HMDHP from dihydroneopterin triphosphate in vitro and has been proposed to provide a bypass to the FolB step in vivo. Bacterial genes encoding PTPS-like proteins with active-site glutamate, cysteine, or both residues were accordingly tested together with the P. falciparum gene for complementation of the Escherichia coli folB mutation. The P. falciparum sequence and bacterial sequences with glutamate or glutamate plus cysteine were active; those with cysteine alone were not. These results demonstrate that PTPS paralogs with an active-site glutamate (designated PTPS-III proteins) can functionally replace FolB in vivo. Recombinant bacterial PTPS-III proteins, like the P. falciparum enzyme, mediated conversion of dihydroneopterin triphosphate to HMDHP, but other PTPS proteins did not. Neither PTPS-III nor other PTPS proteins exhibited significant dihydroneopterin aldolase activity. Phylogenetic analysis indicated that PTPS-III proteins may have arisen independently in various PTPS lineages. Consistent with this possibility, merely introducing a glutamate residue into the active site of a PTPS protein conferred incipient activity in the growth complementation assay, and replacing glutamate with alanine in a PTPS-III protein abolished complementation.
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Gottier, Petra, Mauro Serricchio, Rita Vitale, Angela Corcelli, and Peter Buetikofer. "Cross-species complementation of bacterial- and eukaryotic-type cardiolipin synthases." Microbial Cell 4, no. 11 (November 6, 2017): 376–83. http://dx.doi.org/10.15698/mic2017.11.598.

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Kraemer, Susanne A., and Gregory J. Velicer. "Social complementation and growth advantages promote socially defective bacterial isolates." Proceedings of the Royal Society B: Biological Sciences 281, no. 1781 (April 22, 2014): 20140036. http://dx.doi.org/10.1098/rspb.2014.0036.

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Social interactions among diverse individuals that encounter one another in nature have often been studied among animals but rarely among microbes. For example, the evolutionary forces that determine natural frequencies of bacteria that express cooperative behaviours at low levels remain poorly understood. Natural isolates of the soil bacterium Myxococcus xanthus sampled from the same fruiting body often vary in social phenotypes, such as group swarming and multicellular development. Here, we tested whether genotypes highly proficient at swarming or development might promote the persistence of less socially proficient genotypes from the same fruiting body. Fast-swarming strains complemented slower isolates, allowing the latter to keep pace with faster strains in mixed groups. During development, one low-sporulating strain was antagonized by high sporulators, whereas others with severe developmental defects had those defects partially complemented by high-sporulating strains. Despite declining in frequency overall during competition experiments spanning multiple cycles of development, developmentally defective strains exhibited advantages during the growth phases of competitions. These results suggest that microbes with low-sociality phenotypes often benefit from interacting with more socially proficient strains. Such complementation may combine with advantages at other traits to increase equilibrium frequencies of low-sociality genotypes in natural populations.
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Valencia-Burton, Maria, Ron M. McCullough, Charles R. Cantor, and Natalia E. Broude. "RNA visualization in live bacterial cells using fluorescent protein complementation." Nature Methods 4, no. 5 (April 1, 2007): 421–27. http://dx.doi.org/10.1038/nmeth1023.

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Green, Michael R., and Joseph Sambrook. "Screening Bacterial Colonies Using X-Gal and IPTG: α-Complementation." Cold Spring Harbor Protocols 2019, no. 12 (December 2019): pdb.prot101329. http://dx.doi.org/10.1101/pdb.prot101329.

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Sambrook, Joseph, and David W. Russell. "Screening Bacterial Colonies Using X-gal and IPTG: α-Complementation." Cold Spring Harbor Protocols 2006, no. 1 (June 2006): pdb.prot3945. http://dx.doi.org/10.1101/pdb.prot3945.

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Dissertations / Theses on the topic "Bacterial complementation"

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Löfdahl, Per-Åke. "On bacterial formats in protein library technology." Doctoral thesis, KTH, Molekylär Bioteknologi, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-10993.

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Millions of years of evolution have resulted in an immense number of different proteins, which participate in virtually every process within cells and thus are of utmost importance for allknown forms of life. In addition, there are several examples of natural proteins which have found use in applications outside their natural environment, such as the use of enzymes infood industry and washing powders or the use of antibodies in diagnostic, bioseparation or therapeutic applications. To improve the performance of proteins in such applications, anumber of techniques, all collectively referred to as ‘protein engineering’, are performed in thelaboratory.Traditionally, methods involving ‘rational design’, where a few alterations are introduced atspecific protein locations to hopefully result in expected improvements have been applied.However, the use of more recent techniques involving a simultaneous construction of a large number of candidate variants (protein libraries) by various diversification principles, fromwhich rare clones showing enhanced properties can be isolated have contributed greatly to thefield of protein engineering.In the present thesis, different protein traits of biotechnological importance have beenaddressed for improvements by the use of such methods, in which there is a crucial need tomaintain a clonal link between the genotype and the phenotype to allow an identification of protein library members isolated by virtue of their functional properties. In all protein library investigations included in this thesis this coupling has been obtained by Escherichia coli bacterialcell-membrane compartmental confinement.In a first study, a combination of error prone PCR and gene-shuffling was applied to the Tobacco Etch Virus (TEV)-protease gene in order to produce collections from which genesencoding variants showing an enhanced soluble expression of the enzyme frequently used inbiotechnology to cleave fusion proteins were identified. Using Green Fluorescence Protein(GFP)-based cell fluorescence analysis, a clone with a five-fold increase in the yield of solubly produced protein was successfully isolated. In a second study, a novel and different GFPbased selection system, in addition also involving targeted in vivo protein degradation principles,was employed for investigations of the substrate sequence space of the same protease. In two additional studies, a selection system denoted Protein Fragment Complementation Assay(PCA), based on the affinity driven structural complementation of a genetically split β-lactamase enzyme was used to identify variants having desired target protein binding abilities,including both specificity and affinity. Using Darwinian principles concerning clonal growth advantages, affibody binding proteins showing sub-nanomolar dissociation constants to thehuman cytokine TNF-α were isolated. Taken together, these studies have shown that the bacterial format is very well suited for use in various aspects of protein library selection.
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Linscott, Kristin Brooke. "DISCOVERING A NOVEL ANTIFUNGAL TARGET IN DOWNSTREAM STEROL BIOSYNTHESIS USING A SQUALENE SYNTHASE FUNCTIONAL MOTIF." UKnowledge, 2017. http://uknowledge.uky.edu/biochem_etds/33.

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The sterol biosynthetic pathway is essential for growth of all eukaryotic cells and the main target of antifungal agents. The emergence of resistance to these antifungals in an already ill patient population indicates a need to develop drugs that have a broad spectrum of activity among pathogenic fungi and have minimal patient toxicity. Squalene synthase is the first committed step in the sterol pathway and has been studied intensively for development of antifungal agents. While the overall architecture of this enzyme is identical throughout eukaryotes, it was shown that plant and animal genes cannot complement a squalene synthase knockout mutation in yeast unless the carboxy-terminal domain is swapped for one of fungal origin. This implies that there is a component of the fungal carboxy-terminal domain that is responsible for the complementation phenotype and that is unique to the fungal kingdom of life. To determine the role of the carboxy-terminal domain of squalene synthase in the sterol pathway, we used the yeast Saccharomyces cerevisiae with a squalene synthase knockout mutation and expressed squalene synthases originating from fungi, plants, and animals. In contrast to previous observations, all enzymes tested could partially complement the knockout mutation when the genes were weakly expressed. When induced, non-fungal squalene synthases could not complement the knockout mutation and instead led to the accumulation of carboxysterol intermediates, suggesting an interaction between squalene synthase and the downstream sterol C4-decarboxylase. Overexpression of a sterol C4-decarboxylase from any kingdom of life both decreased the accumulation of carboxysterol intermediates and allowed non-fungal squalene synthases to complement the squalene synthase knockout mutation. Using chimeric squalene synthases from each kingdom of life, the motif in the C-terminal domain responsible for preventing this toxicity was mapped to a kingdom-specific 26-amino acid hinge motif adjacent to the catalytic domain. Furthermore, over-expression of the carboxy-terminal domain alone containing a hinge motif from fungi, not from animals or plants, led to growth inhibition of wild-type yeast. Since this hinge region is unique to and highly conserved within each kingdom of life, this data provides evidence for the development of an antifungal therapeutic as well as for tools to develop an understanding of triterpene catalytic activity and identify similar motifs in other biosynthetic pathways.
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Butler, Kate Ann. "Functional complementation of ΔexbD E. coli by homologous exbD genes." Bowling Green State University / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1377012630.

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Johnson, Kenyetta Alicia. "Extending chemical complemenation to bacteria and furthering nuclear receptor based protein engineering and drug discovery." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/29652.

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Thesis (Ph.D)--Chemistry and Biochemistry, Georgia Institute of Technology, 2009.
Committee Chair: Doyle, Donald; Committee Member: Barry, Bridgette; Committee Member: Bommarius, Andreas; Committee Member: Ledoux, Joe; Committee Member: Matsumura, Ichiro; Committee Member: Oyelere, Adegboyega. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Allibert, Patrice. "Clonage et caractérisation d'un gène de Escherichia coli complémentant une mutation de type ntr chez Rhodopseudomonas capsulata." Grenoble 1, 1986. http://www.theses.fr/1986GRE10079.

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Vacek, Vojtěch. "Syntéza železo-sirných center v Monocercomonoides exilis." Doctoral thesis, 2020. http://www.nusl.cz/ntk/nusl-437064.

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In the search for the mitochondrion of oxymonads, DNA of Monocercomonoides exilis - an oxymonad isolated from the gut of Chinchilla, was isolated and its genome was sequenced. Sequencing resulted in a fairly complete genome which was extensively searched or genes for mitochondrion related proteins, but no reliable candidate for such gene was identified. Even genes for the ISC pathway, which is responsible for Fe-S cluster assembly and considered to be the only essential function of reduced mitochondrion-like organelles (MROs), were absent. Instead, we were able to detect the presence of a SUF pathway which functionally replaced the ISC pathway. Closer examination of the SUF pathway based on heterologous localisation revealed that this pathway localised in the cytosol. In silico analysis showed that SUF genes are highly conserved at the level of secondary and tertiary structure and most catalytic residues and motifs are present in their sequences. The functionality of these proteins was further indirectly confirmed by complementation experiments in Escherichia coli where SUF proteins of M. exilis were able to restore at least partially Fe-S cluster assembly of strains deficient in the SUF and ISC pathways. We also proved by bacterial adenylate cyclase two-hybrid system that SufB and SufC can form...
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Book chapters on the topic "Bacterial complementation"

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Coplin, D. L., R. D. Frederick, D. Majerczak, and E. Haas. "Complementation of Avirulent Mutants of Erwinia Stewartii by Recombinant Plasmids." In Plant Pathogenic Bacteria, 413–18. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3555-6_82.

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Lee, Lan-Ying, and Stanton B. Gelvin. "Bimolecular Fluorescence Complementation for Imaging Protein Interactions in Plant Hosts of Microbial Pathogens." In Host-Bacteria Interactions, 185–208. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1261-2_11.

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Nakahara, Masaaki, Akihiko Hattori, Carl E. Bauer, and Kazuhito Inoue. "Functional Complementation of Protochlorophyllide Reductase Activity in Mutants of Rhodobacter Capsulatus by Introduction of a Genomic Library from Green Nonsulfur Bacterium Chloroflexus Aurantiacus." In Photosynthesis: Mechanisms and Effects, 2873–76. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_673.

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Wurst, Wolfgang, and Achim Gossler. "Gene trap strategies in ES cells." In Gene Targeting. Oxford University Press, 1999. http://dx.doi.org/10.1093/oso/9780199637928.003.0010.

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Gene trap (GT) strategies in mouse embryonic stem (ES) cells are increasingly being used for detecting patterns of gene expression (1-4, isolating and mutating endogenous genes (5-7), and identifying targets of signalling molecules and transcription factors (3, 8-10). The general term gene trap refers to the random integration of a reporter gene construct (called entrapment vector) (11, 12) into the genome such that ‘productive’ integration events bring the reporter gene under the transcriptional regulation of an endogenous gene. In some cases this also simultaneously generates an insertional mutation. Entrapment vectors were originally developed in bacteria (13), and applied in Drosophila to identify novel developmental genes and/or regulatory sequences (14-17). Subsequently, a modified strategy was developed for mouse in which the reporter gene mRNA becomes fused to an endogenous transcript. Such ‘gene trap’ vectors were initially used primarily as a tool to discover genes involved in development (1, 2,18). In the last five years there has been a significant shift of GT approaches in mouse to much broader, large scale applications in the context of the analysis of mammalian genomes and ‘functional genomics’. Sequencing and physical mapping of both the human and mouse genomes is expected to be completed within the next five years. Already, a large number of mouse and human genes have been identified as expressed sequence tags (ESTs), and very likely the majority of genes will be discovered as ESTs shortly. This vast sequence information contrasts with a rather limited understanding of the in vivo functions of these genes. Whereas DNA sequence can provide some indication of the potential functions of these genes and their products, their physiological roles in the organism have to be determined by mutational analysis. Thus, the sequencing effort of the human genome project has to be complemented by efficient functional analyses of the identified genes. One potentially powerful complementation to the efforts of the human genome project would be a strategy whereby large scale random mutagenesis in mouse is combined with the rapid identification of the mutated genes (6,7,19, and German gene trap consortium, W. W. unpublished data).
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