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Journal articles on the topic 'Bacterial Proteins Thermus thermophilus'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

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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2

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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3

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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4

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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5

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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7

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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9

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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11

Kasai, Koji, Tomoyasu Nishizawa, Kosaku Takahashi, Takeshi Hosaka, Hiroyuki Aoki, and Kozo Ochi. "Physiological Analysis of the Stringent Response Elicited in an Extreme Thermophilic Bacterium, Thermus thermophilus." Journal of Bacteriology 188, no. 20 (2006): 7111–22. http://dx.doi.org/10.1128/jb.00574-06.

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ABSTRACT Guanosine tetraphosphate (ppGpp) is a key mediator of stringent control, an adaptive response of bacteria to amino acid starvation, and has thus been termed a bacterial alarmone. Previous X-ray crystallographic analysis has provided a structural basis for the transcriptional regulation of RNA polymerase activity by ppGpp in the thermophilic bacterium Thermus thermophilus. Here we investigated the physiological basis of the stringent response by comparing the changes in intracellular ppGpp levels and the rate of RNA synthesis in stringent (rel +; wild type) and relaxed (relA and relC;

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12

Zafra, Olga, Felipe Cava, Francis Blasco, Axel Magalon, and Jose Berenguer. "Membrane-Associated Maturation of the Heterotetrameric Nitrate Reductase of Thermus thermophilus." Journal of Bacteriology 187, no. 12 (2005): 3990–96. http://dx.doi.org/10.1128/jb.187.12.3990-3996.2005.

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ABSTRACT The nar operon, coding for the respiratory nitrate reductase of Thermus thermophilus (NRT), encodes a di-heme b-type (NarJ) and a di-heme c-type (NarC) cytochrome. The role of both cytochromes and that of a putative chaperone (NarJ) in the synthesis and maturation of NRT was studied. Mutants of T. thermophilus lacking either NarI or NarC synthesized a soluble form of NarG, suggesting that a putative NarCI complex constitutes the attachment site for the enzyme. Interestingly, the NarG protein synthesized by both mutants was inactive in nitrate reduction and misfolded, showing that memb

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13

Friedrich, Alexandra, Thomas Hartsch, and Beate Averhoff. "Natural Transformation in Mesophilic and Thermophilic Bacteria: Identification and Characterization of Novel, Closely Related Competence Genes in Acinetobacter sp. Strain BD413 andThermus thermophilus HB27." Applied and Environmental Microbiology 67, no. 7 (2001): 3140–48. http://dx.doi.org/10.1128/aem.67.7.3140-3148.2001.

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ABSTRACT The mesophile Acinetobacter sp. strain BD413 and the extreme thermophile Thermus thermophilus HB27 display high frequencies of natural transformation. In this study we identified and characterized a novel competence gene in Acinetobacter sp. strain BD413, comA, whose product displays significant similarities to the competence proteins ComA and ComEC inNeisseria and Bacillus species. Transcription of comA correlated with growth phase-dependent transcriptional regulation of the recently identified pilin-like factors of the transformation machinery. This finding strongly suggests that co

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14

Karuppiah, Vijaykumar, and Jeremy P. Derrick. "Structure of the PilM-PilN Inner Membrane Type IV Pilus Biogenesis Complex from Thermus thermophilus." Journal of Biological Chemistry 286, no. 27 (2011): 24434–42. http://dx.doi.org/10.1074/jbc.m111.243535.

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Type IV pili are surface-exposed filaments, which extend from a variety of bacterial pathogens and play a major role in pathogenesis, motility, and DNA uptake. Here, we present the crystal structure of a complex between a cytoplasmic component of the type IV pilus biogenesis system from Thermus thermophilus, PilM, in complex with a peptide derived from the cytoplasmic portion of the inner membrane protein PilN. PilM also binds ATP, and its structure is most similar to the actin-like protein FtsA. PilN binds in a narrow channel between the 1A and 1C subdomains in PilM; the binding site is well

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15

De Tarafder, Arindam, Narayan Prasad Parajuli, Soneya Majumdar, Betül Kaçar, and Suparna Sanyal. "Kinetic Analysis Suggests Evolution of Ribosome Specificity in Modern Elongation Factor-Tus from “Generalist” Ancestors." Molecular Biology and Evolution 38, no. 8 (2021): 3436–44. http://dx.doi.org/10.1093/molbev/msab114.

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Abstract It has been hypothesized that early enzymes are more promiscuous than their extant orthologs. Whether or not this hypothesis applies to the translation machinery, the oldest molecular machine of life, is not known. Efficient protein synthesis relies on a cascade of specific interactions between the ribosome and the translation factors. Here, using elongation factor-Tu (EF-Tu) as a model system, we have explored the evolution of ribosome specificity in translation factors. Employing presteady state fast kinetics using quench flow, we have quantitatively characterized the specificity of

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16

Jalasvuori, Matti, Silja T. Jaatinen, Simonas Laurinavičius, et al. "The Closest Relatives of Icosahedral Viruses of Thermophilic Bacteria Are among Viruses and Plasmids of the Halophilic Archaea." Journal of Virology 83, no. 18 (2009): 9388–97. http://dx.doi.org/10.1128/jvi.00869-09.

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ABSTRACT We have sequenced the genome and identified the structural proteins and lipids of the novel membrane-containing, icosahedral virus P23-77 of Thermus thermophilus. P23-77 has an ∼17-kb circular double-stranded DNA genome, which was annotated to contain 37 putative genes. Virions were subjected to dissociation analysis, and five protein species were shown to associate with the internal viral membrane, while three were constituents of the protein capsid. Analysis of the bacteriophage genome revealed it to be evolutionarily related to another Thermus phage (IN93), archaeal Halobacterium p

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Chopin, Marie-Christine, Annette Rouault, S. Dusko Ehrlich, and Michel Gautier. "Filamentous Phage Active on the Gram-Positive Bacterium Propionibacterium freudenreichii." Journal of Bacteriology 184, no. 7 (2002): 2030–33. http://dx.doi.org/10.1128/jb.184.7.2030-2033.2002.

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ABSTRACT We present the first description of a single-stranded DNA filamentous phage able to replicate in a gram-positive bacterium. Phage B5 infects Propionibacterium freudenreichii and has a genome consisting of 5,806 bases coding for 10 putative open reading frames. The organization of the genome is very similar to the organization of the genomes of filamentous phages active on gram-negative bacteria. The putative coat protein exhibits homology with the coat proteins of phages PH75 and Pf3 active on Thermus thermophilus and Pseudomonas aeruginosa, respectively. B5 is, therefore, evolutionar

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McDonald, John H. "Patterns of Temperature Adaptation in Proteins from the Bacteria Deinococcus radiodurans and Thermus thermophilus." Molecular Biology and Evolution 18, no. 5 (2001): 741–49. http://dx.doi.org/10.1093/oxfordjournals.molbev.a003856.

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Moncja, Kristi, and Michael W. Van Dyke. "Determination and Dissection of DNA-Binding Specificity for the Thermus thermophilus HB8 Transcriptional Regulator TTHB099." International Journal of Molecular Sciences 21, no. 21 (2020): 7929. http://dx.doi.org/10.3390/ijms21217929.

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Transcription factors (TFs) have been extensively researched in certain well-studied organisms, but far less so in others. Following the whole-genome sequencing of a new organism, TFs are typically identified through their homology with related proteins in other organisms. However, recent findings demonstrate that structurally similar TFs from distantly related bacteria are not usually evolutionary orthologs. Here we explore TTHB099, a cAMP receptor protein (CRP)-family TF from the extremophile Thermus thermophilus HB8. Using the in vitro iterative selection method Restriction Endonuclease Pro

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Kurpe, S. R., S. Yu Grishin, A. V. Glyakina, et al. "Antibacterial effects of peptides synthesized based on the sequence of ribosome protein S1." Biomeditsinskaya Khimiya 67, no. 3 (2021): 231–43. http://dx.doi.org/10.18097/pbmc20216703231.

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Antibiotic resistance of bacteria is a topical problem on a global scale. Sometimes vigorous human activity leads to an increase in the number of bacteria carrying resistance genes in the environment. Antimicrobial peptides (AMPs) and similar compounds are potential candidates for combating antibiotic-resistant bacteria. Previously, we proposed and successfully tested on Thermus thermophilus a new mechanism of AMP action. This mechanism of directed coaggregation is based on the interaction of a peptide capable of forming fibrils with a target protein. In this work, we discuss the criteria for

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Ribble, Wendy, Shawn D. Kane, and James M. Bullard. "Long-Range PCR Amplification of DNA by DNA Polymerase III Holoenzyme from Thermus thermophilus." Enzyme Research 2015 (January 19, 2015): 1–16. http://dx.doi.org/10.1155/2015/837842.

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DNA replication in bacteria is accomplished by a multicomponent replicase, the DNA polymerase III holoenzyme (pol III HE). The three essential components of the pol III HE are the α polymerase, the β sliding clamp processivity factor, and the DnaX clamp-loader complex. We report here the assembly of the functional holoenzyme from Thermus thermophilus (Tth), an extreme thermophile. The minimal holoenzyme capable of DNA synthesis consists of α, β and DnaX (τ and γ), δ and δ′ components of the clamp-loader complex. The proteins were each cloned and expressed in a native form. Each component of th

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Manyumwa, Colleen Varaidzo, and Özlem Tastan Bishop. "In Silico Investigation of Potential Applications of Gamma Carbonic Anhydrases as Catalysts of CO2 Biomineralization Processes: A Visit to the Thermophilic Bacteria Persephonella hydrogeniphila, Persephonella marina, Thermosulfidibacter takaii, and Thermus thermophilus." International Journal of Molecular Sciences 22, no. 6 (2021): 2861. http://dx.doi.org/10.3390/ijms22062861.

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Carbonic anhydrases (CAs) have been identified as ideal catalysts for CO2 sequestration. Here, we report the sequence and structural analyses as well as the molecular dynamics (MD) simulations of four γ-CAs from thermophilic bacteria. Three of these, Persephonella marina, Persephonella hydrogeniphila, and Thermosulfidibacter takaii originate from hydrothermal vents and one, Thermus thermophilus HB8, from hot springs. Protein sequences were retrieved and aligned with previously characterized γ-CAs, revealing differences in the catalytic pocket residues. Further analysis of the structures follow

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Sazanov, Leonid A., Rozbeh Baradaran, Rouslan G. Efremov, John M. Berrisford, and Gurdeep Minhas. "A long road towards the structure of respiratory complex I, a giant molecular proton pump." Biochemical Society Transactions 41, no. 5 (2013): 1265–71. http://dx.doi.org/10.1042/bst20130193.

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Complex I (NADH:ubiquinone oxidoreductase) is central to cellular energy production, being the first and largest enzyme of the respiratory chain in mitochondria. It couples electron transfer from NADH to ubiquinone with proton translocation across the inner mitochondrial membrane and is involved in a wide range of human neurodegenerative disorders. Mammalian complex I is composed of 44 different subunits, whereas the ‘minimal’ bacterial version contains 14 highly conserved ‘core’ subunits. The L-shaped assembly consists of hydrophilic and membrane domains. We have determined all known atomic s

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Grishin, Sergei Y., Evgeniya I. Deryusheva, Andrey V. Machulin, et al. "Amyloidogenic Propensities of Ribosomal S1 Proteins: Bioinformatics Screening and Experimental Checking." International Journal of Molecular Sciences 21, no. 15 (2020): 5199. http://dx.doi.org/10.3390/ijms21155199.

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Structural S1 domains belong to the superfamily of oligosaccharide/oligonucleotide-binding fold domains, which are highly conserved from prokaryotes to higher eukaryotes and able to function in RNA binding. An important feature of this family is the presence of several copies of the structural domain, the number of which is determined in a strictly limited range from one to six. Despite the strong tendency for the aggregation of several amyloidogenic regions in the family of the ribosomal S1 proteins, their fibril formation process is still poorly understood. Here, we combined computational an

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Wang, Shipeng, Misaki Ogata, Shoichiro Horita, Jun Ohtsuka, Koji Nagata, and Masaru Tanokura. "A novel six-coordinated ferric ion binding mode of TtFbpA." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C483. http://dx.doi.org/10.1107/s2053273314095163.

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Iron is an essential element for the growth and survival of nearly all living organisms. However, it is difficult for most organisms to get enough iron from the environment, because of the extremely low solubility of ferric ion. One of the strategies for iron acquisition is to use the ATP-binding cassette (ABC) transport system. In Gram-negative bacteria, a typical iron uptake ABC transporter consists of a ferric ion-binding protein (Fbp) located in periplasm (FbpA), two transmembrane proteins that form a pathway for ferric ions (FbpB), and two peripheral ATP-binding proteins located at the cy

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Chen, Chih-Wei, Julia A. Pavlova, Dmitrii A. Lukianov, et al. "Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome." Antibiotics 10, no. 4 (2021): 390. http://dx.doi.org/10.3390/antibiotics10040390.

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Chloramphenicol (CHL) is a ribosome-targeting antibiotic that binds to the peptidyl transferase center (PTC) of the bacterial ribosome and inhibits peptide bond formation. As an approach for modifying and potentially improving the properties of this inhibitor, we explored ribosome binding and inhibitory properties of a semi-synthetic triphenylphosphonium analog of CHL—CAM-C4-TPP. Our data demonstrate that this compound exhibits a ~5-fold stronger affinity for the bacterial ribosome and higher potency as an in vitro protein synthesis inhibitor compared to CHL. The X-ray crystal structure of the

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Olson, Matthew W., Alexey Ruzin, Eric Feyfant, Thomas S. Rush, John O'Connell, and Patricia A. Bradford. "Functional, Biophysical, and Structural Bases for Antibacterial Activity of Tigecycline." Antimicrobial Agents and Chemotherapy 50, no. 6 (2006): 2156–66. http://dx.doi.org/10.1128/aac.01499-05.

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ABSTRACT Tigecycline is a novel glycylcycline antibiotic that possesses broad-spectrum activity against many clinically relevant species of bacterial pathogens. The mechanism of action of tigecycline was delineated using functional, biophysical, and molecular modeling experiments in this study. Functional assays showed that tigecycline specifically inhibits bacterial protein synthesis with potency 3- and 20-fold greater than that of minocycline and tetracycline, respectively. Biophysical analyses demonstrated that isolated ribosomes bind tigecycline, minocycline, and tetracycline with dissocia

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Blesa, Alba, Carolina Elvira César, Beate Averhoff, and José Berenguer. "Noncanonical Cell-to-Cell DNA Transfer in Thermus spp. Is Insensitive to Argonaute-Mediated Interference." Journal of Bacteriology 197, no. 1 (2014): 138–46. http://dx.doi.org/10.1128/jb.02113-14.

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Horizontal gene transfer drives the rapid evolution of bacterial populations. Classical processes that promote the lateral flow of genetic information are conserved throughout the prokaryotic world. However, some species have nonconserved transfer mechanisms that are not well known. This is the case for the ancient extreme thermophileThermus thermophilus. In this work, we show thatT. thermophilusstrains are capable of exchanging large DNA fragments by a novel mechanism that requires cell-to-cell contacts and employs components of the natural transformation machinery. This process facilitates t

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Eyler, Daniel E., Monika K. Franco, Zahra Batool, et al. "Pseudouridinylation of mRNA coding sequences alters translation." Proceedings of the National Academy of Sciences 116, no. 46 (2019): 23068–74. http://dx.doi.org/10.1073/pnas.1821754116.

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Chemical modifications of RNAs have long been established as key modulators of nonprotein-coding RNA structure and function in cells. There is a growing appreciation that messenger RNA (mRNA) sequences responsible for directing protein synthesis can also be posttranscriptionally modified. The enzymatic incorporation of mRNA modifications has many potential outcomes, including changing mRNA stability, protein recruitment, and translation. We tested how one of the most common modifications present in mRNA coding regions, pseudouridine (Ψ), impacts protein synthesis using a fully reconstituted ba

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Navas, Laura Emilce, Mónica Florin-Christensen, Graciela Beatriz Benintende, Rubén Oreste Zandomeni, and Marcelo Facundo Berretta. "Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities." Journal of Molecular Microbiology and Biotechnology 28, no. 3 (2018): 99–106. http://dx.doi.org/10.1159/000491698.

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Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain <i>Thermus</i> sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this typ

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Garber, M. B., S. Ch Agalarov, I. A. Eliseikina, et al. "Ribosomal proteins from Thermus thermophilus for structural investigations." Biochimie 74, no. 4 (1992): 327–36. http://dx.doi.org/10.1016/0300-9084(92)90110-z.

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Thomas, Torsten, Naresh Kumar, and Ricardo Cavicchioli. "Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens." Journal of Bacteriology 183, no. 6 (2001): 1974–82. http://dx.doi.org/10.1128/jb.183.6.1974-1982.2001.

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ABSTRACT Low-temperature-adapted archaea are abundant in the environment, yet little is known about the thermal adaptation of their proteins. We have previously compared elongation factor 2 (EF-2) proteins from Antarctic (Methanococcoides burtonii) and thermophilic (Methanosarcina thermophila) methanogens and found that theM. burtonii EF-2 had greater intrinsic activity at low temperatures and lower thermal stability at high temperatures (T. Thomas and R. Cavicchioli, J. Bacteriol. 182:1328–1332, 2000). While the gross thermal properties correlated with growth temperature, the activity and sta

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Chevance, Fabienne F. V., Marc Erhardt, Christina Lengsfeld, Sung-Jae Lee, and Winfried Boos. "Mlc of Thermus thermophilus: a Glucose-Specific Regulator for a Glucose/Mannose ABC Transporter in the Absence of the Phosphotransferase System." Journal of Bacteriology 188, no. 18 (2006): 6561–71. http://dx.doi.org/10.1128/jb.00715-06.

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ABSTRACT We report the presence of Mlc in a thermophilic bacterium. Mlc is known as a global regulator of sugar metabolism in gram-negative enteric bacteria that is controlled by sequestration to a glucose-transporting EIIGlc of the phosphotransferase system (PTS). Since thermophilic bacteria do not possess PTS, Mlc in Thermus thermophilus must be differently controlled. DNA sequence alignments between Mlc from T. thermophilus (MlcTth) and Mlc from E. coli (MlcEco) revealed that MlcTth conserved five residues of the glucose-binding motif of glucokinases. Here we show that MlcTth is not a gluco

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Cameron, Dale M., Steven T. Gregory, Jill Thompson, Moo-Jin Suh, Patrick A. Limbach, and Albert E. Dahlberg. "Thermus thermophilus L11 Methyltransferase, PrmA, Is Dispensable for Growth and Preferentially Modifies Free Ribosomal Protein L11 Prior to Ribosome Assembly." Journal of Bacteriology 186, no. 17 (2004): 5819–25. http://dx.doi.org/10.1128/jb.186.17.5819-5825.2004.

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ABSTRACT The ribosomal protein L11 in bacteria is posttranslationally trimethylated at multiple amino acid positions by the L11 methyltransferase PrmA, the product of the prmA gene. The role of L11 methylation in ribosome function or assembly has yet to be determined, although the deletion of Escherichia coli prmA has no apparent phenotype. We have constructed a mutant of the extreme thermophile Thermus thermophilus in which the prmA gene has been disrupted with the htk gene encoding a heat-stable kanamycin adenyltransferase. This mutant shows no growth defects, indicating that T. thermophilus

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Hidalgo, Aurelio, Lorena Betancor, Renata Moreno, et al. "Thermus thermophilus as a Cell Factory for the Production of a Thermophilic Mn-Dependent Catalase Which Fails To Be Synthesized in an Active Form in Escherichia coli." Applied and Environmental Microbiology 70, no. 7 (2004): 3839–44. http://dx.doi.org/10.1128/aem.70.7.3839-3844.2004.

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ABSTRACT Thermostable Mn-dependent catalases are promising enzymes in biotechnological applications as H2O2-detoxifying systems. We cloned the genes encoding Mn-dependent catalases from Thermus thermophilus HB27 and HB8 and a less thermostable mutant carrying two amino acid replacements (M129V and E293G). When the wild-type and mutant genes were overexpressed in Escherichia coli, unmodified or six-His-tagged proteins of the expected size were overproduced as inactive proteins. Several attempts to obtain active forms or to activate the overproduced proteins were unsuccessful, even when soluble

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Tamakoshi, Masatada, Akihiko Yamagishi, and Tairo Oshima. "Screening of stable proteins in an extreme thermophile, Thermus thermophilus." Molecular Microbiology 16, no. 5 (1995): 1031–36. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02328.x.

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Yusupov, M. M., and T. N. Spirina. "Accessibility of ribosomal proteins to trypsin in Thermus thermophilus ribosomes." Biopolymers and Cell 6, no. 4 (1990): 65–69. http://dx.doi.org/10.7124/bc.00027f.

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Friedrich, Alexandra, Judit Rumszauer, Anke Henne, and Beate Averhoff. "Pilin-Like Proteins in the Extremely Thermophilic Bacterium Thermus thermophilus HB27: Implication in Competence for Natural Transformation and Links to Type IV Pilus Biogenesis." Applied and Environmental Microbiology 69, no. 7 (2003): 3695–700. http://dx.doi.org/10.1128/aem.69.7.3695-3700.2003.

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ABSTRACT The extreme thermophile Thermus thermophilus HB27 exhibits high frequencies of natural transformation. Although we recently reported identification of the first competence genes in Thermus, the molecular basis of DNA uptake is unknown. A pilus-like structure is assumed to be involved. Twelve genes encoding prepilin-like proteins were identified in three loci in the genome of T. thermophilus. Mutational analyses, described in this paper, revealed that one locus, which contains four genes that encode prepilin-like proteins (pilA1 to pilA4), is essential for natural transformation. Addit

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Nishida, Hiromi, and Makoto Nishiyama. "Evolution of Lysine Biosynthesis in the Phylum Deinococcus-Thermus." International Journal of Evolutionary Biology 2012 (May 8, 2012): 1–6. http://dx.doi.org/10.1155/2012/745931.

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Thermus thermophilus biosynthesizes lysine through the α-aminoadipate (AAA) pathway: this observation was the first discovery of lysine biosynthesis through the AAA pathway in archaea and bacteria. Genes homologous to the T. thermophilus lysine biosynthetic genes are widely distributed in bacteria of the Deinococcus-Thermus phylum. Our phylogenetic analyses strongly suggest that a common ancestor of the Deinococcus-Thermus phylum had the ancestral genes for bacterial lysine biosynthesis through the AAA pathway. In addition, our findings suggest that the ancestor lacked genes for lysine biosynt

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Katsani, K. R., P. Tsiboli, K. Anagnostopoulos, H. Urlaub, and T. Choli-Papadopoulou. "Identification of the 50S Ribosomal Proteins from the Eubacterium Thermus thermophilus." Biological Chemistry 381, no. 11 (2000): 1079–87. http://dx.doi.org/10.1515/bc.2000.133.

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Abstract The total protein mixture from the 50S subunit (TP-50) of the eubacterium Thermus thermophilus was characterized after blotting onto PVDF membranes from two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and sequencing. The proteins were numbered according to their primary structure similarity with their counterparts from other species. One of them has been marked with an asterisk, namely L*23, because unlike the other known ribosomal proteins it shows a very low degree of homology. A highly acidic 5S rRNA binding protein, TL5, was characterized and compared with the availab

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Sedelnikova, S. E., O. S. Shikaeva, N. K. Avlijakulov, et al. "Proteins of the Thermus thermophilus ribosome. Purification of proteins from the large ribosomal subunit." Biochimie 76, no. 5 (1994): 440–51. http://dx.doi.org/10.1016/0300-9084(94)90121-x.

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Teague, Josiah L., John K. Barrows, Cynthia A. Baafi, and Michael W. Van Dyke. "Discovering the DNA-Binding Consensus of the Thermus thermophilus HB8 Transcriptional Regulator TTHA1359." International Journal of Molecular Sciences 22, no. 18 (2021): 10042. http://dx.doi.org/10.3390/ijms221810042.

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Transcription regulatory proteins, also known as transcription factors, function as molecular switches modulating the first step in gene expression, transcription initiation. Cyclic-AMP receptor proteins (CRPs) and fumarate and nitrate reduction regulators (FNRs) compose the CRP/FNR superfamily of transcription factors, regulating gene expression in response to a spectrum of stimuli. In the present work, a reverse-genetic methodology was applied to the study of TTHA1359, one of four CRP/FNR superfamily transcription factors in the model organism Thermus thermophilus HB8. Restriction Endonuclea

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Fujino, Yasuhiro, Yuko Nagayoshi, Makoto Iwase, Takushi Yokoyama, Toshihisa Ohshima, and Katsumi Doi. "Silica-Induced Protein (Sip) in Thermophilic Bacterium Thermus thermophilus Responds to Low Iron Availability." Applied and Environmental Microbiology 82, no. 11 (2016): 3198–207. http://dx.doi.org/10.1128/aem.04027-15.

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ABSTRACTThermus thermophilusHB8 expresses silica-induced protein (Sip) when cultured in medium containing supersaturated silicic acids. Using genomic information, Sip was identified as a Fe3+-binding ABC transporter. Detection of a 1-kb hybridized band in Northern analysis revealed thatsiptranscription is monocistronic and thatsiphas its own terminator and promoter. The sequence of thesippromoter showed homology with that of the σA-dependent promoter, which is known as a housekeeping promoter in HB8. Considering thatsipis transcribed when supersaturated silicic acids are added, the existence o

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Tsiboli, Paraskevi, Elke Herfurth, and Theodora Choli. "Purification and Characterization of the 30S Ribosomal Proteins from the Bacterium Thermus thermophilus." European Journal of Biochemistry 226, no. 1 (2008): 169–77. http://dx.doi.org/10.1111/j.1432-1033.1994.0t169.x.

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Tsiboli, Paraskevi, Elke Herfurth, and Theodora Choli. "Purification and Characterization of the 30S Ribosomal Proteins from the Bacterium Thermus thermophilus." European Journal of Biochemistry 226, no. 1 (1994): 169–77. http://dx.doi.org/10.1111/j.1432-1033.1994.tb20038.x.

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Gongadze, G., I. Kashparov, S. Lorenz, et al. "5S rRNA binding ribosomal proteins from Thermus thermophilus : identification and some structural properties." FEBS Letters 386, no. 2-3 (1996): 260–62. http://dx.doi.org/10.1016/0014-5793(96)00457-7.

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Kondo, Naoyuki, Akio Ebihara, Heng Ru, et al. "Thermus thermophilus-derived protein tags that aid in preparation of insoluble viral proteins." Analytical Biochemistry 385, no. 2 (2009): 278–85. http://dx.doi.org/10.1016/j.ab.2008.10.050.

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Sedelnikova, S. E., S. C. Agalarov, M. B. Garber, and M. M. Yusupov. "Proteins of the Thermus thermophilus ribosome Purification of several individual proteins and crystallization of protein TL7." FEBS Letters 220, no. 1 (1987): 227–30. http://dx.doi.org/10.1016/0014-5793(87)80910-9.

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Fridjonsson, Olafur, та Ralf Mattes. "Production of Recombinant α-Galactosidases inThermus thermophilus". Applied and Environmental Microbiology 67, № 9 (2001): 4192–98. http://dx.doi.org/10.1128/aem.67.9.4192-4198.2001.

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ABSTRACT A Thermus thermophilus selector strain for production of thermostable and thermoactive α-galactosidase was constructed. For this purpose, the native α-galactosidase gene (agaT) ofT. thermophilus TH125 was inactivated to prevent background activity. In our first attempt, insertional mutagenesis ofagaT by using a cassette carrying a kanamycin resistance gene led to bacterial inability to utilize melibiose (α-galactoside) and galactose as sole carbohydrate sources due to a polar effect of the insertional inactivation. A Gal+ phenotype was assumed to be essential for growth on melibiose.

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Bricio, Carlos, Laura Alvarez, Manuel J. Gómez, and José Berenguer. "Partial and complete denitrification in Thermus thermophilus: lessons from genome drafts." Biochemical Society Transactions 39, no. 1 (2011): 249–53. http://dx.doi.org/10.1042/bst0390249.

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We have obtained draft genomic sequences of PD (partial denitrificant) and CD (complete denitrificant) strains of Thermus thermophilus. Their genomes are similar in size to that of the aerobic strains sequenced to date and probably contain a similar megaplasmid. In the CD strain, the genes encoding a putative cytochrome cd1 Nir (nitrite reductase) and ancillary proteins were clustered with a cytochrome c-dependent Nor (nitric oxide reductase), and with genes that are probably implicated in their regulation. The Nar (nitrate reductase) and associated genes were also clustered and located 7 kb d

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