Biochemical characterization and homology modeling of a purine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus: Insights into mechanisms of protein stabilization

2009 ◽  
Vol 483 (1) ◽  
pp. 55-65 ◽  
Author(s):  
Marina Porcelli ◽  
Iolanda Peluso ◽  
Anna Marabotti ◽  
Angelo Facchiano ◽  
Giovanna Cacciapuoti
Keyword(s):  
Homology Modeling ◽  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Protein Stabilization

scholarly journals Pyrimidine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus- biochemical characterization and homology modeling

FEBS Journal ◽  
2008 ◽  
Vol 275 (8) ◽  
pp. 1900-1914 ◽  
Author(s):  
Marina Porcelli ◽  
Luigi Concilio ◽  
Iolanda Peluso ◽  
Anna Marabotti ◽  
Angelo Facchiano ◽  
...  
Keyword(s):  
Homology Modeling ◽  
Biochemical Characterization ◽  
Sulfolobus Solfataricus

scholarly journals A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus

2007 ◽  
Vol 408 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Mariarita De Felice ◽  
Valentina Aria ◽  
Luca Esposito ◽  
Mariarosaria De Falco ◽  
Biagio Pucci ◽  
...  
Keyword(s):  
High Efficiency ◽  
Biochemical Characterization ◽  
Sequence Similarity ◽  
Sulfolobus Solfataricus ◽  
Genetic Material ◽  
Dna Helicase ◽  
Soluble Form ◽  
Monomeric Form ◽  
Genome Database ◽  
Strand Annealing

To protect their genetic material cells adopt different mechanisms linked to DNA replication, recombination and repair. Several proteins function at the interface of these DNA transactions. In the present study, we report on the identification of a novel archaeal DNA helicase. BlastP searches of the Sulfolobus solfataricus genome database allowed us to identify an open reading frame (SSO0112, 875 amino acid residues) having sequence similarity with the human RecQ5β. The corresponding protein, termed Hel112 by us, was produced in Escherichia coli in soluble form, purified to homogeneity and characterized. Gel-filtration chromatography and glycerol-gradient sedimentation analyses revealed that Hel112 forms monomers and dimers in solution. Biochemical characterization of the two oligomeric species revealed that only the monomeric form has an ATP-dependent 3′–5′ DNA-helicase activity, whereas, unexpectedly, both the monomeric and dimeric forms possess DNA strand-annealing capability. The Hel112 monomeric form is able to unwind forked and 3′-tailed DNA structures with high efficiency, whereas it is almost inactive on blunt-ended duplexes and bubble-containing molecules. This analysis reveals that S. solfataricus Hel112 shares some enzymatic features with the RecQ-like DNA helicases and suggests potential cellular functions of this protein.

Hyperthermophilic flavin reductase from Sulfolobus solfataricus P2: Production and biochemical characterization

2019 ◽  
Vol 66 (6) ◽  
pp. 915-923
Author(s):  
Gokhan Gun ◽  
Rahmi Imamoglu ◽  
Ozge Tatli ◽  
Yuda Yurum ◽  
Ahmet Tarik Baykal ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Flavin Reductase

Biochemical characterization and mutational improvement of a thermophilic esterase from Sulfolobus solfataricus P2

2010 ◽  
Vol 32 (8) ◽  
pp. 1151-1157 ◽  
Author(s):  
Yu-Shuan Shang ◽  
Xian-En Zhang ◽  
Xu-De Wang ◽  
Yong-Chao Guo ◽  
Zhi-Ping Zhang ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Thermophilic Esterase

scholarly journals Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus

1998 ◽  
Vol 335 (2) ◽  
pp. 441-447 ◽  
Author(s):  
Maria Rosaria FARAONE-MENNELLA ◽  
Agata GAMBACORTA ◽  
Barbara NICOLAUS ◽  
Benedetta FARINA
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Enzymic Activity ◽  
Sds Page ◽  
Thermophilic Archaeon ◽  
Displacement Assay ◽  
Elongation Step ◽  
Ph Range ◽  
Good Agreement

A poly(ADP-ribose) polymerase-like enzyme, detected in a crude homogenate from Sulfolobus solfataricus by means of activity and immunoblot analyses, was purified to electrophoretic homogeneity by a rapid procedure including two sequential affinity chromatographies, on NAD+-agarose and DNA-Sepharose. The latter column selected specifically the poly(ADP-ribosyl)ating enzyme with a 17% recovery of enzymic activity and a purification of more than 15000-fold. The molecular mass (54–55 kDa) assessed by SDS/PAGE and immunoblot was definitely lower than that determined for the corresponding eukaryotic protein. The enzyme was proved to be thermophilic, with a temperature optimum of approx. 80 °C, and thermostable, with a half-life of 204 min at 80 °C, in good agreement with the requirements of a thermozyme. It displayed a Km towards NAD+ of 154±50 µM; in the pH range 6.5–10.0 the activity values were similar, not showing a real optimum pH. The enzyme was able to bind homologous DNA, as evidenced by the ethidium bromide displacement assay. The product of the ADP-ribosylating reaction co-migrated with the short oligomers of ADP-ribose (less than 6 residues) from a eukaryotic source. Reverse-phase HPLC analysis of the products, after digestion with phosphodiesterase I, gave an elution profile reproducing that obtained by the enzymic digestion of the rat testis poly(ADP-ribose). These results strongly suggest that the activities of the purified enzyme include the elongation step.

Biochemical characterization and homology modeling of polyamine oxidase from cyanobacterium Synechocystis sp. PCC 6803

2017 ◽  
Vol 119 ◽  
pp. 159-169 ◽  
Author(s):  
Khanittha Samasil ◽  
Leonor Lopes de Carvalho ◽  
Pirkko Mäenpää ◽  
Tiina A. Salminen ◽  
Aran Incharoensakdi
Keyword(s):  
Homology Modeling ◽  
Biochemical Characterization ◽  
Polyamine Oxidase ◽  
Synechocystis Sp ◽  
Pcc 6803

Biochemical characterization of two Cdc6/ORC1-like proteins from the crenarchaeon Sulfolobus solfataricus

Extremophiles ◽  
2005 ◽  
Vol 10 (1) ◽  
pp. 61-70 ◽  
Author(s):  
Mariarita De Felice ◽  
Luca Esposito ◽  
Mosè Rossi ◽  
Francesca M. Pisani
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus

Molecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus

Extremophiles ◽  
2001 ◽  
Vol 5 (3) ◽  
pp. 183-192 ◽  
Author(s):  
Anna d' Abusco ◽  
Sergio Ammendola ◽  
Roberto Scandurra ◽  
Laura Politi
Keyword(s):  
Biochemical Characterization ◽  
Sulfolobus Solfataricus ◽  
Hyperthermophilic Archaeon
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