Relevant bibliographies by topics / Bacterial Proteins Thermus thermophilus

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Academic literature on the topic 'Bacterial Proteins Thermus thermophilus'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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Journal articles on the topic "Bacterial Proteins Thermus thermophilus"

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Kurpe, Stanislav, Sergei Grishin, Alexey Surin, et al. "Antimicrobial and Amyloidogenic Activity of Peptides Synthesized on the Basis of the Ribosomal S1 Protein from Thermus Thermophilus." International Journal of Molecular Sciences 21, no. 17 (2020): 6382. http://dx.doi.org/10.3390/ijms21176382.

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Controlling the aggregation of vital bacterial proteins could be one of the new research directions and form the basis for the search and development of antibacterial drugs with targeted action. Such approach may be considered as an alternative one to antibiotics. Amyloidogenic regions can, like antibacterial peptides, interact with the “parent” protein, for example, ribosomal S1 protein (specific only for bacteria), and interfere with its functioning. The aim of the work was to search for peptides based on the ribosomal S1 protein from T. thermophilus, exhibiting both aggregation and antibact
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Shinkai, Akeo, Satoshi Kira, Noriko Nakagawa, Aiko Kashihara, Seiki Kuramitsu, and Shigeyuki Yokoyama. "Transcription Activation Mediated by a Cyclic AMP Receptor Protein from Thermus thermophilus HB8." Journal of Bacteriology 189, no. 10 (2007): 3891–901. http://dx.doi.org/10.1128/jb.01739-06.

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ABSTRACT The extremely thermophilic bacterium Thermus thermophilus HB8, which belongs to the phylum Deinococcus-Thermus, has an open reading frame encoding a protein belonging to the cyclic AMP (cAMP) receptor protein (CRP) family present in many bacteria. The protein named T. thermophilus CRP is highly homologous to the CRP family proteins from the phyla Firmicutes, Actinobacteria, and Cyanobacteria, and it forms a homodimer and interacts with cAMP. CRP mRNA and intracellular cAMP were detected in this strain, which did not drastically fluctuate during cultivation in a rich medium. The expres
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Friedrich, Alexandra, Christina Prust, Thomas Hartsch, Anke Henne, and Beate Averhoff. "Molecular Analyses of the Natural Transformation Machinery and Identification of Pilus Structures in the Extremely Thermophilic Bacterium Thermus thermophilus Strain HB27." Applied and Environmental Microbiology 68, no. 2 (2002): 745–55. http://dx.doi.org/10.1128/aem.68.2.745-755.2002.

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ABSTRACT Thermus thermophilus HB27, an extremely thermophilic bacterium, exhibits high competence for natural transformation. To identify genes of the natural transformation machinery of T. thermophilus HB27, we performed homology searches in the partially completed T. thermophilus genomic sequence for conserved competence genes. These analyses resulted in the detection of 28 open reading frames (ORFs) exhibiting significant similarities to known competence proteins of gram-negative and gram-positive bacteria. Disruption of 15 selected potential competence genes led to the identification of 8
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Czyz, Agata, and Grzegorz Wegrzyn. "The Obg subfamily of bacterial GTP-binding proteins: essential proteins of largely unknown functions that are evolutionarily conserved from bacteria to humans." Acta Biochimica Polonica 52, no. 1 (2005): 35–43. http://dx.doi.org/10.18388/abp.2005_3483.

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Members of the Obg subfamily of small GTP-binding proteins (called Obg, CgtA, ObgE or YhbZ in different bacterial species) have been found in various prokaryotic and eukaryotic organisms, ranging from bacteria to humans. Although serious changes in phenotypes are observed in mutant bacteria devoid of Obg or its homologues, specific roles of these GTP-binding proteins remain largely unknown. Recent genetic and biochemical studies, as well as determination of the structures of Obg proteins from Bacillus subtilis and Thermus thermophilus, shed new light on the possible functions of the members of
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Nesper, Jutta, Alexander Brosig, Philippe Ringler, et al. "Omp85Tt from Thermus thermophilus HB27: an Ancestral Type of the Omp85 Protein Family." Journal of Bacteriology 190, no. 13 (2008): 4568–75. http://dx.doi.org/10.1128/jb.00369-08.

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ABSTRACT Proteins belonging to the Omp85 family are involved in the assembly of β-barrel outer membrane proteins or in the translocation of proteins across the outer membrane in bacteria, mitochondria, and chloroplasts. The cell envelope of the thermophilic bacterium Thermus thermophilus HB27 is multilayered, including an outer membrane that is not well characterized. Neither the precise lipid composition nor much about integral membrane proteins is known. The genome of HB27 encodes one Omp85-like protein, Omp85Tt, representing an ancestral type of this family. We overexpressed Omp85Tt in T. t
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Chiba, Yoko, Kenro Oshima, Hiroyuki Arai, Masaharu Ishii, and Yasuo Igarashi. "Discovery and Analysis of Cofactor-dependent Phosphoglycerate Mutase Homologs as Novel Phosphoserine Phosphatases in Hydrogenobacter thermophilus." Journal of Biological Chemistry 287, no. 15 (2012): 11934–41. http://dx.doi.org/10.1074/jbc.m111.330621.

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Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of phosphoserine to serine and inorganic phosphate. PSPs, which have been found in all three domains of life, belong to the haloacid dehalogenase-like hydrolase superfamily. However, certain organisms, particularly bacteria, lack a classical PSP gene, although they appear to possess a functional phosphoserine synthetic pathway. The apparent lack of a PSP ortholog in Hydrogenobacter thermophilus, an obligately chemolithoautotrophic and thermophilic bacterium, represented a missing link in serine anabolism because our previous study
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Burkhardt, Janin, Janet Vonck, and Beate Averhoff. "Structure and Function of PilQ, a Secretin of the DNA Transporter from the Thermophilic Bacterium Thermus thermophilus HB27." Journal of Biological Chemistry 286, no. 12 (2011): 9977–84. http://dx.doi.org/10.1074/jbc.m110.212688.

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Secretins are a family of large bacterial outer membrane protein complexes mediating the transport of complex structures, such as type IV pili, DNA and filamentous phage, or various proteins, such as extracellular enzymes and pathogenicity determinants. PilQ of the thermophilic bacterium Thermus thermophilus HB27 is a member of the secretin family required for natural transformation. Here we report the isolation, structural, and functional analyses of a unique PilQ from T. thermophilus. Native PAGE, gel filtration chromatography, and electrophoretic mobility shift analyses indicated that PilQ
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Leontiadou, Fotini, Dimitra Triantafillidou, and Theodora Choli-Papadopoulou. "On the Characterization of the Putative S20-Thx Operon of Thermus thermophilus." Biological Chemistry 382, no. 7 (2001): 1001–6. http://dx.doi.org/10.1515/bc.2001.126.

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Abstract A putative operon of the ribosomal proteins S20 and Thx has been determined in a 1.4 kb sequenced region of T. thermophilus genomic DNA. Both genes have a promoter sequence 29 nt upstream of ORF1, possess their own ShineDalgarno motifs (GGAG) and are separated by only 9 nucleotides, a feature characteristic of the compact Thermus thermophilus genome. This is a novel arrangement, since Thx is unique to the Thermus bacteria and in all other prokaryotes the S20 gene is monocistronic. Our results, in conjunction with the recent finding that Thx is located on the top of the head of the 30S
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Killeavy, Erin E., Gerwald Jogl, and Steven T. Gregory. "Tiamulin-Resistant Mutants of the Thermophilic Bacterium Thermus thermophilus." Antibiotics 9, no. 6 (2020): 313. http://dx.doi.org/10.3390/antibiotics9060313.

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Tiamulin is a semisynthetic pleuromutilin antibiotic that binds to the 50S ribosomal subunit A site and whose (((2-diethylamino)ethyl)thio)-acetic acid tail extends into the P site to interfere with peptide bond formation. We have isolated spontaneous tiamulin-resistant mutants of the thermophilic bacterium Thermus thermophilus, containing either single amino acid substitutions in ribosomal protein uL3 or single base substitutions in the peptidyltransferase active site of 23S rRNA. These mutations are consistent with those found in other organisms and are in close proximity to the crystallogra
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Plotka, Magdalena, Anna-Karina Kaczorowska, Aleksandra Stefanska, et al. "Novel Highly Thermostable Endolysin from Thermus scotoductus MAT2119 Bacteriophage Ph2119 with Amino Acid Sequence Similarity to Eukaryotic Peptidoglycan Recognition Proteins." Applied and Environmental Microbiology 80, no. 3 (2013): 886–95. http://dx.doi.org/10.1128/aem.03074-13.

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ABSTRACTIn this study, we present the discovery and characterization of a highly thermostable endolysin from bacteriophage Ph2119 infectingThermusstrain MAT2119 isolated from geothermal areas in Iceland. Nucleotide sequence analysis of the 16S rRNA gene affiliated the strain with the speciesThermus scotoductus. Bioinformatics analysis has allowed identification in the genome of phage 2119 of an open reading frame (468 bp in length) coding for a 155-amino-acid basic protein with anMrof 17,555. Ph2119 endolysin does not resemble any known thermophilic phage lytic enzymes. Instead, it has conserv
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Dissertations / Theses on the topic "Bacterial Proteins Thermus thermophilus"

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Ronchetti, Mirco Fabio. "Funktionelle Analyse des Na+(Li+)/H+-Austauschers CPA2 aus dem thermophilen Bakterium Thermus thermophilus /." [S.l.] : [s.n.], 2009. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000281105.

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Pöltl, Dominik. "Charakterisierung des putativen Außenmembran-Proteins TTC0322 von Thermus thermophilus." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-23805.

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Beinker, Philipp [Verfasser]. "Untersuchungen zur Struktur und Funktion des Proteins ClpB aus Thermus thermophilus / vorgelegt von Philipp Beinker." 2003. http://d-nb.info/969462816/34.

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Brosig, Alexander [Verfasser]. "X-ray crystallographic analysis of three membrane proteins : the nicotinic acetylcholine receptor from Torpedo californica, Omp85 and TtoA from Thermus thermophilus HB27 / presented by Alexander Brosig." 2009. http://d-nb.info/995347751/34.

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Kanaujia, Shankar Prasad. "Structural Studies On Bovine Pancreatic Phospholipase A2 And Proteins Involved In Molybdenum Cofactor Biosynthesis." Thesis, 2010. http://etd.iisc.ernet.in/handle/2005/2000.

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We have carried out structural studies on bovine pancreatic phospholipase A2 (BPLA2) and two proteins involved in molybdenum cofactor (Moco) biosynthesis pathway. In addition, molecular-dynamics simulations and other analyses have been performed to corroborate the findings obtained from the crystal structures. Crystal structures of the three active-site mutants (H48N, D49N and D49K) of BPLA2 were determined to understand the mechanism by which the mutant H48N is able to catalyze the reaction of phospholipid hydrolysis and to see the effect of the loss of Ca 2+ ion in the active site of D49N a
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Book chapters on the topic "Bacterial Proteins Thermus thermophilus"

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Bergquist, P. L., and K. M. Borges. "Thermus thermophilus HB8." In Bacterial Genomes. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-6369-3_84.

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Lasa, Iñigo, José R. Castón, Luis A. Fernández-Herrero, et al. "Phenotypic, Biochemical, and Structural Analysis of “S-layer” Mutants from Thermus thermophilus HB8." In Bacterial Growth and Lysis. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9359-8_12.

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Peter, Marcus E., and Mathias Sprinzl. "Affinity Labeling of the GDP/GTP Binding Site in Thermus Thermophilus Elongation Factor Tu." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_10.

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Mather, M. W., P. Springer, and J. A. Fee. "Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases." In The Molecular Basis of Bacterial Metabolism. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75969-7_10.

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Agalarov, Sultan, Marat Yusupov, and Gulnara Yusupova. "Reconstitution of Functionally Active Thermus thermophilus 30S Ribosomal Subunit from Ribosomal 16S RNA and Ribosomal Proteins." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2763-0_19.

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