MthTrpY also represses transcription of the remotely located trpB2, which encodes a homolog of the β subunit of tryptophan synthases, in a concentration-dependent manner both in the absence or presence of tryptophan (Karr et al., 2008; Xie & Reeve, 2005). Sulfolobus acidocaldarius has three unique enzymes that allow the organism to grow on carbon sources. coli shuttle vectors are very stable in hosts which make them suitable for the use in protein expression and reporter gene studies [5]. The stoichiometric binding of reverse gyrase to nicked circular duplex DNA in the absence of ATP results in a decrease of linking number of at least – 0.5 turn per molecule after covalent closure (Jaxel et al., 1989). FEBS Lett. The S. acidocaldarius reverse gyrase activity is not detectable below 60°C and is optimal at 75°C. To occupy such an extreme environment efficiently, Sulfolobus acidocaldarius has unique features which allow them to live in hot and acidic springs. Shotgun sequencing was used to map the genome for Sulfolobus acidocaldarious strain DSM639. The preference for Mn2+ over Mg2+ is explained by the histidine ligands. [37] where they showed that Fe-S cluster was not required for global stability of the protein, single-strand DNA binding or ATPase activity, but was necessary for helicase activity. Due to the high similarity in SaXPD midpoint redox potentials with MutY and EndoIII, one could hypothesize that XPD shuttles electrons to and from MutY and EndoIII in vitro. A number of in vivo and in vitro studies have examined regulation of tryptophan biosynthesis in M. thermautotrophicus (Mth) (Cafasso et al., 2010; Čuboňovà et al., 2007; Karr, Sandman, Lurz, & Reeve, 2008; Xie & Reeve, 2005). [61]. After verifying that the pyrE mutation in PBL4001 was responsible for the uracil auxotrophic phenotype, this cell line was used as a host for further genetic manipulations in M. sedula. species: Thermoplasma volcanium. Purified thermopsin cannot be stained by Coomassie Blue or commonly used protein dyes after SDS–PAGE. George Rice, Kenneth Stedman, Jamie Snyder, Blake Wiedenheft, Debbie Willits, Susan Brumfield, Timothy McDermott, and Mark J. Sulfolobus is a genus of microorganism in the family Sulfolobaceae. Thermopsin is an acid protease produced by a thermophilic archaeon, Sulfolobus acidocaldarius. They are capable of direct removal of DNA damage, base excision repair, nucleotide excision repair, and homolog-dependent double-strand-break repair [1]. Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) Furthermore, motility away from lethal hot spots is observed, even in the absence of carbon and energy source [2]. This species was found to grow optimally between 75 and 80 … Y81A and Y81G gave larger amounts of HexPP and GFPP than did Y81S. However, transcription was only repressed from the trpY promoter (Čuboňovà et al., 2007; Karr et al., 2008). Barton’s group has proposed that these Fe-S clusters are redox-active and used to scan the genome for damage and communicate with other repair proteins via charge transport [55–57]. Sulpholobus acidocaldarius is an aerobic thermoacidophilic crenarchaeon which grows optimally at 80C and pH 2 in terrestrial solfataric springs ( 1) Habitat ( 1) Primarily aquatic. When acidic springs are absent, solfatara soils and mud pots (due to the microbial oxidation of sulfuric acid) are heated by rising streams to various temperatures [3]. As the distance is similar to the length of the hydrocarbon moiety of FPP, it is suggested that the aromatic ring of Tyr81 might prevent further chain elongations longer than C15. Sulfolobus acidocaldarius strain B12 is known to be a viral host [7]. Biophysical Journal, September 2005. Two MthTrpY variants, A128E and G149R, were commonly recovered in the mutant screen. Thermopsin hydrolyzes many proteins, which are all potential substrates for assay. Sulfolobus acidocaldarius stirs high interests with its low mutation rate at high temperature environment with its strong efficient repair systems [1]. These includes a homolog of the bacterial enzyme to degrade poly(3-hydroxyalkanotes), a special transporter for malate and other C4-dicarboxylates, and two subunits of an aromatic ring dioxygenase to degrade simple aromatic ring compounds [1]. These results indicate that the mutated enzymes can catalyze the chain elongation beyond FPP. They reported polyphosphate kinase (PPK) activities could not be reproduced in 2001. The DNA helicase substrate used in the assay comprised of 20-mer double-stranded DNA duplex with 9-mer single-stranded overhang on the 5′ and 3′ end. To be able to survive, mechanisms to adapt to or counteract these threats have been developed by microbes. Further studies led to the cloning and characterization of the corresponding gene and the results showed glycosyl transferase (GT) activities [9]. The active site geometry is shown in Figure 26. S. acidocaldarius was the first Sulfolobus species to be described, in 1972 by Thomas D. Brock and collaborators. D.C. Weatherburn, ... L.F. Lindoy, in Comprehensive Coordination Chemistry II, 2003. This mutation produced a frameshift leading to a premature stop codon, truncating the normal protein product from 191 to 86 amino acid residues (Maezato et al., 2012). The hyperthermophilic archaeon Sulfolobus acidocaldarius exchanges and recombines chromosomal markers by a conjugational mechanism, and the overall yield of recombinants is greatly increased by previous exposure to UV light. “The Genome of Sulfolobus acidocaldarius, A Model Organism of the Crenarchaeota”. Ajay A. Vashisht, James A. Wohlschlegel, in Helicases from All Domains of Life, 2019. A szerzők 2292 fehérje kódoló gént jósolnak. 35(12): e88. Complementation of the pyrE mutation PBL4001 was done using an independently replicating pJLacS plasmid (pBN1090) containing the S. solfataricus pyrEF genes, and transformants of PBL4001 were recovered by selection for uracil prototrophy (Maezato et al., 2012). The new vector system will facilitate the genetic studies of Sulfolobus, as well as other biotechnological uses, including overexpression and optimization of thermophilic enzymes that are not readily performed in mesophilic hosts [5]. possess a great metabolic versatility and grow heterotrophically on various carbon sources, such as different sugars and peptides.

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