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 Mr 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 the 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.
An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus / P. Fusi, M. Grisa, G. Tedeschi, A. Negri, A. Guerritore, P. Tortora. - In: FEBS LETTERS. - ISSN 0014-5793. - 360:2(1995), pp. 187-190.
|Titolo:||An 8.5-kDa ribonuclease from the extreme thermophilic archaebacterium Sulfolobus solfataricus|
|Parole Chiave:||Archaebacterium; DNA-binding protein; Ribonuclease; Sulfolobus solfataricus; Thermophilic|
|Settore Scientifico Disciplinare:||Settore BIO/10 - Biochimica|
|Data di pubblicazione:||1995|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1016/0014-5793(95)00098-T|
|Appare nelle tipologie:||01 - Articolo su periodico|