Identification of the Essential Catalytic Residues and Selectivity-Related Residues of Maltooligosyltrehalose Trehalohydrolase from the Thermophilic Archaeon Sulfolobus solfataricus ATCC 35092

2008 ◽  
Vol 56 (14) ◽  
pp. 5628-5633 ◽  
Author(s):  
Tsuei-Yun Fang ◽  
Wen-Chi Tseng ◽  
Tong-Yuan Shih ◽  
Mei-Ying Wang
Keyword(s):  
Sulfolobus Solfataricus ◽  
Catalytic Residues ◽  
Thermophilic Archaeon

A thioredoxin from the extreme thermophilic Archaeon Sulfolobus solfataricus

1994 ◽  
Vol 26 (3) ◽  
pp. 375-380 ◽  
Author(s):  
Annamaria Guagliardi ◽  
Valentina Nobile ◽  
Simonetta Bartolucci ◽  
Mose' Rossi
Keyword(s):  
Sulfolobus Solfataricus ◽  
Thermophilic Archaeon

The thermophilic archaeon Sulfolobus solfataricus is able to grow on phenol

2005 ◽  
Vol 156 (5-6) ◽  
pp. 677-689 ◽  
Author(s):  
Viviana Izzo ◽  
Eugenio Notomista ◽  
Alessandra Picardi ◽  
Francesca Pennacchio ◽  
Alberto Di Donato
Keyword(s):  
Sulfolobus Solfataricus ◽  
Thermophilic Archaeon

Gene content and organization of a 281-kbp contig from the genome of the extremely thermophilic archaeon,Sulfolobus solfataricusP2

Genome ◽  
2000 ◽  
Vol 43 (1) ◽  
pp. 116-136 ◽  
Author(s):  
Robert L Charlebois ◽  
Rama K Singh ◽  
Christina C.-Y Chan-Weiher ◽  
Ghislaine Allard ◽  
Cynthia Chow ◽  
...  
Keyword(s):  
Sulfolobus Solfataricus ◽  
Genome Project ◽  
Trna Genes ◽  
Insertion Sequences ◽  
Key Words Archaea ◽  
Ribosomal Protein Genes ◽  
Arginine Biosynthesis ◽  
Histidine Biosynthesis ◽  
Thermophilic Archaeon ◽  
Lipopolysaccharide Biosynthesis

The sequence of a 281-kbp contig from the crenarchaeote Sulfolobus solfataricus P2 was determined and analysed. Notable features in this region include 29 ribosomal protein genes, 12 tRNA genes (four of which contain archaeal-type introns), operons encoding enzymes of histidine biosynthesis, pyrimidine biosynthesis, and arginine biosynthesis, an ATPase operon, numerous genes for enzymes of lipopolysaccharide biosynthesis, and six insertion sequences. The content and organization of this contig are compared with sequences from crenarchaeotes, euryarchaeotes, bacteria, and eukaryotes. Key words: Archaea, Sulfolobus Genome Project, comparative genomics, bioinformatics.

The Molecular Chaperonin TF55 from the Thermophilic Archaeon Sulfolobus solfataricus

1994 ◽  
Vol 242 (4) ◽  
pp. 397-407 ◽  
Author(s):  
Stefan Knapp ◽  
Ingeborg Schmidt-Krey ◽  
Hans Hebert ◽  
Tomas Bergman ◽  
Hans Jörnvall ◽  
...  
Keyword(s):  
Sulfolobus Solfataricus ◽  
Thermophilic Archaeon

scholarly journals In Vitro Processing of the 16S rRNA of the Thermophilic Archaeon Sulfolobus solfataricus

2001 ◽  
Vol 183 (13) ◽  
pp. 3866-3874 ◽  
Author(s):  
Andrea Ciammaruconi ◽  
Paola Londei
Keyword(s):  
16S Rrna ◽  
Sulfolobus Solfataricus ◽  
Conserved Sequence ◽  
Processing Enzymes ◽  
Cell Extracts ◽  
In Vitro Processing ◽  
16S Rna ◽  
Thermophilic Archaeon ◽  
Rna Maturation

ABSTRACT In this paper we have analyzed the processing in vitro of the 16S rRNA of the thermophilic archaeon Sulfolobus solfataricus, using pre-rRNA substrates transcribed in vitro and different protein preparations as the source of processing enzymes. We show that the 5′ external transcribed spacer of the S. solfataricus pre-rRNA transcript contains a target site for a specific endonuclease, which recognizes a conserved sequence also existing in the early A0 and 0 processing sites of Saccharomyces cerevisiae and vertebrates. This site is present in other members of the kingdomCrenarchaeota but apparently not in theEuryarchaeota. Furthermore, S. solfataricuspre-16S RNA is processed within the double-helical stem formed by the inverted repeats flanking the 16S RNA sequence, in correspondence with a bulge-helix-bulge motif. The endonuclease responsible for this cleavage is present in both the Crenarchaeota and theEuryarchaeota. The processing pattern remained the same when the substrate was a 30S ribonucleoprotein particle instead of the naked RNA. Maturation of either the 5′ or the 3′ end of the 16S RNA molecule was not observed, suggesting either that maturation requires conditions not easily reproducible in vitro or that the responsible endonucleases are scarcely represented in cell extracts.

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