Protein p3, a ribonuclease we previously isolated from the archaebacterium Sulfolobus solfataricus [P. Fusi et al. (1993) Eur. J. Biochem, 211, 305-310], was subjected to complete amino acid sequencing, It consisted of 75 residues, with a calculated M(r) of 8582, a pI of 10.1, and had some degree of monomethylation at Lys-4 and Lys-6, p2, a previously sequenced, 62-residue ribonuclease from tbe same organism, had an identical sequence for 57 consecutive residues starting from the N-terminus. p2 and p3 also showed a striking similarity to five other proteins previously isolated from Sulfolobus strains and identified as DNA-binding proteins, However, the C-terminus, 10 residue region of p3 did not show any similarity to these proteins; in contrast, it was significantly similar to stretches in three eubacterial ribonucleases from Bacillus strains. No difference between p2 and p3 has so far been detected as regards their catalytic properties, Available data suggest that these molecules have a narrow substrate specificity and probably play specific roles in RNA processing

Fusi, P., Grisa, M., Tedeschi, G., Negri, A., Guerritore, A., Tortora, P. (1995). An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus. FEBS LETTERS, 360(2), 187-190 [10.1016/0014-5793(95)00098-T].

An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus

FUSI, PAOLA ALESSANDRA;
1995

Abstract

Protein p3, a ribonuclease we previously isolated from the archaebacterium Sulfolobus solfataricus [P. Fusi et al. (1993) Eur. J. Biochem, 211, 305-310], was subjected to complete amino acid sequencing, It consisted of 75 residues, with a calculated M(r) of 8582, a pI of 10.1, and had some degree of monomethylation at Lys-4 and Lys-6, p2, a previously sequenced, 62-residue ribonuclease from tbe same organism, had an identical sequence for 57 consecutive residues starting from the N-terminus. p2 and p3 also showed a striking similarity to five other proteins previously isolated from Sulfolobus strains and identified as DNA-binding proteins, However, the C-terminus, 10 residue region of p3 did not show any similarity to these proteins; in contrast, it was significantly similar to stretches in three eubacterial ribonucleases from Bacillus strains. No difference between p2 and p3 has so far been detected as regards their catalytic properties, Available data suggest that these molecules have a narrow substrate specificity and probably play specific roles in RNA processing
Articolo in rivista - Articolo scientifico
Archaebacterium; DNA-binding protein; Ribonuclease; Sulfolobus solfataricus; Thermophilic;
English
1995
360
2
187
190
none
Fusi, P., Grisa, M., Tedeschi, G., Negri, A., Guerritore, A., Tortora, P. (1995). An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus. FEBS LETTERS, 360(2), 187-190 [10.1016/0014-5793(95)00098-T].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/15676
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