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Thermus aquaticus strain:YT-1

ABSTRACT: Thermus aquaticus strain:YT-1 Genome sequencing and assembly

PROVIDER: PRJNA291648 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	LHCI01.dat.gz	Other
	LHCI01.fasta.gz	Fasta.gz
	LHCI01.master.dat	Other
	LHCI01.dat.gz	Other

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Thermus aquaticus strain:YT-1

Project description:Thermus aquaticus strain:YT-1 Genome sequencing and assembly

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Expression profile of crp-deficient Thermus thermophilus HB8 strain

Project description:We observed the expression profile of the total mRNA of crp (TTHA1437) deletion mutant of Thermus thermophilus HB8 strain grown in a rich (TT) medium at 70 degC

2010-10-15 | GSE21459 | GEO

miRNA expression profiles in YT and NK92 cells

Project description:The miRNA expression profiles of of EBV-infected YT and NK92 cells are compared. YT cells have weaker expression of T-bet and IFNg than NK92 cells. It was found that the EBV-encoded miR-BART20-5p inhibits the expression of T-bet and IFNg in YT cells.

2014-01-21 | GSE53476 | GEO

TTHB212 (anti-sigmaE)-deficient Thermus thermophilus HB8 strain: time course

Project description:We observed the expression profile of the total mRNA of TTHB212-deficient of Thermus thermophilus HB8 strain grown in a rich medium at 70°C for 7 and 8 hours

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The third restriction-modification system from Thermus aquaticus YT-1: solving the riddle of two TaqII specificities.

Project description:Two restriction-modification systems have been previously discovered in Thermus aquaticus YT-1. TaqI is a 263-amino acid (aa) Type IIP restriction enzyme that recognizes and cleaves within the symmetric sequence 5'-TCGA-3'. TaqII, in contrast, is a 1105-aa Type IIC restriction-and-modification enzyme, one of a family of Thermus homologs. TaqII was originally reported to recognize two different asymmetric sequences: 5'-GACCGA-3' and 5'-CACCCA-3'. We previously cloned the taqIIRM gene, purified the recombinant protein from Escherichia coli, and showed that TaqII recognizes the 5'-GACCGA-3' sequence only. Here, we report the discovery, isolation, and characterization of TaqIII, the third R-M system from T. aquaticus YT-1. TaqIII is a 1101-aa Type IIC/IIL enzyme and recognizes the 5'-CACCCA-3' sequence previously attributed to TaqII. The cleavage site is 11/9 nucleotides downstream of the A residue. The enzyme exhibits striking biochemical similarity to TaqII. The 93% identity between their aa sequences suggests that they have a common evolutionary origin. The genes are located on two separate plasmids, and are probably paralogs or pseudoparalogs. Putative positions and aa that specify DNA recognition were identified and recognition motifs for 6 uncharacterized Thermus-family enzymes were predicted.

| S-EPMC5587805 | biostudies-literature

Highly conserved salt bridge stabilizes a proteinase K subfamily enzyme, Aqualysin I, from Thermus aquaticus YT-1.

Project description:The proteinase K subfamily enzymes, thermophilic Aqualysin I (AQN) from Thermus aquaticus YT-1 and psychrophilic serine protease (VPR) from Vibrio sp. PA-44, have six and seven salt bridges, respectively. To understand the possible significance of salt bridges in the thermal stability of AQN, we prepared mutant proteins in which amino acid residues participating in salt bridges common to proteinase K subfamily members and intrinsic to AQN were replaced to disrupt the bridges one at a time. Disruption of a salt bridge common to proteinase K subfamily enzymes in the D183N mutant resulted in a significant reduction in thermal stability, and a massive change in the content of the secondary structure was observed, even at 70°C, in the circular dichroism (CD) analysis. These results indicate that the common salt bridge Asp183-Arg12 is important in maintaining the conformation of proteinase K subfamily enzymes and suggest the importance of proximity between the regions around Asp183 and the N-terminal region around Arg12. Of the three mutants that lack an AQN intrinsic salt bridge, D212N was more prone to unfolding at 80°C than the wild-type enzyme. Similarly, D17N and E237Q were less thermostable than the wild-type enzyme, although this may be partially due to increased autolysis. The AQN intrinsic salt bridges appear to confer additional thermal stability to this enzyme. These findings will further our understanding of the factors involved in stabilizing protein structure.

| S-EPMC4131155 | biostudies-literature

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