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BS-RNase tetramers: An example of domain-swapped oligomers (69 visite)

Adinolfi S, Piccoli R, Sica F, Mazzarella L

Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 1996 Dec 2; 398(2-3): 326-332.

Tipo di articolo: Journal Article,

Impact factor: 3.504

Impact factor a 5 anni: 3.304


Parole chiave: Domain Swapping, Oligomeric Structure, Seminal Ribonuclease, Animal Tissue, Article, Cattle, Controlled Study, Enzyme Activity, Enzyme Structure, Molecular Weight, Nonhuman, Priority Journal, Protein Family, Protein Quaternary Structure, Seminal Vesicle, Binding Sites, Biopolymers, Chromatography, High Pressure Liquid, Crystallography, X-Ray, Cytosine Nucleotides, Dimerization, Electrophoresis, Polyacrylamide Gel, Endoribonucleases, Models, Protein Conformation, Protein Structure, Secondary, Tertiary, Fungal, Bos Taurus, Bovinae,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030566834&partnerID=40&md5=9fc0ed057730d9ddd2988eb610ed8998

In the ribonuclease superfamily, dimericity is a unique feature of bovine seminal RNase (BS-RNase). In about two-thirds of native BS-RNase molecules, the two subunits interchange their N-terminal tails, thus generating domain-swapped dimers (MxM), which mostly responsible for enzyme biological activities and allostericity. Higher molecular weight BS-RNase oligomers can also be prepared [Libonati, M. (1969) Ital. J. Biochem. 18, 407-417.]. This paper reports on BS-RNase tetrameric derivatives which were isolated and enzymatically characterized. The data collected and the analysis of the crystal packing of MxM dimers suggested a structural model for tetramer assembly, in which the four subunits are enchained by multiple domain-swapping events.
CNR, Ctro. di Stud. di B., Universita Federico II di Napoli, Via Mezzocannone 4, 80134 Napoli, Italy

Dipto. di Chim. Organica e Biologica, Universita Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
D'Alessio, G., Di Donato, A., Parente, A., Piccoli, R., (1991) Trends Biochem. Sci., 16, pp. 104-10

D'Alessio, G., (1993) Trends Cell. Biol., 3, pp. 106-109

Tamburrini, M., Piccoli, R., De Prisco, R., Di Donato, A., D'Alessio, G., (1986) Ital. J. Biochem., 35, pp. 22-32

Piccoli, R., Di Donato, A., D'Alessio, G., (1988) Biochem. J., 253, pp. 329-336

Piccoli, R., Tamburrini, M., Piccialli, G., Di Donato, A., Parente, A., D'Alessio, G., (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 1870-1874

Mazzarella, L., Capasso, S., Demasi, D., Di Lorenzo, G., Mattia, C.A., Zagari, A., (1993) Acta Crystallogr., D49, pp. 389-402

Fruchter, R.G., Crestfield, A.M., (1965) J. Biol. Chem., 240, pp. 3875-3882

Mazzarella, L., Mattia, C.A., Capasso, S., Di Lorenzo, G., (1987) Gazz. Chim. Ital., 117, pp. 91-97

Cafaro, V., De Lorenzo, C., Piccoli, R., Bracale, A., Mastronicola, M.R., Di Donato, A., D'Alessio, G., (1995) FEBS Lett., 359, pp. 31-34

(1994) Nat. Struct. Biol., 1, pp. 411-412

Bennett, M.J., Schlunegger, M.P., Eisenberg, D., (1995) Protein Sci., 4, pp. 2455-2468

Libonati, M., (1969) Ital. J. Biochem., 18, pp. 407-417

Laemmli, U.K., (1970) Nature, 227, pp. 680-685

Marfey, P.S., Novak, H., Uziel, M., Yphantis, D.A., (1965) J. Biol. Chem., 240, pp. 3264-3269

Kunitz, M., (1946) J. Biol. Chem., 164, pp. 563-568

D'Alessio, G., Malorni, M.C., Parente, A., (1975) Biochemistry, 14, pp. 1116-1121

Teipel, J., Koshland D.E., Jr., (1969) Biochemistry, 9, pp. 3337-3342

Mazzarella, L., Vitagliano, L., Zagari, A., (1995) Proc. Natl. Acad. Sci. USA, 92, pp. 3799-3803

Murthy, B.S., De Lorenzo, C., Piccoli, R., D'Alessio, G., Sirdeshmukh, R., (1996) Biochemistry, 35, pp. 3880-3885

Fruchter, R. G., Crestfield, A. M., (1965) J. Biol. Chem., 240, pp. 3875-3882

(1994) Nat. Struct. Biol., 1, pp. 411-412

Bennett, M. J., Schlunegger, M. P., Eisenberg, D., (1995) Protein Sci., 4, pp. 2455-2468

Laemmli, U. K., (1970) Nature, 227, pp. 680-685

Marfey, P. S., Novak, H., Uziel, M., Yphantis, D. A., (1965) J. Biol. Chem., 240, pp. 3264-3269

Murthy, B. S., De Lorenzo, C., Piccoli, R., D'Alessio, G., Sirdeshmukh, R., (1996) Biochemistry, 35, pp. 3880-3885

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16 Records (16 escludendo Abstract e Conferenze).
Impact factor totale: 64.25 (64.25 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 61.823 (61.823 escludendo Abstract e Conferenze).







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