The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer
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The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer (404 views)

Sica F, Pica A, Merlino A, Russo Krauss I, Ercole C, Picone D

Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2013 Nov 29; 587(23): 3755-3762.

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Paper type: Journal Article,

Impact factor: 3.341, 5-year impact factor: 3.47

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84887989317&partnerID=40&md5=69ab07525e4c7e1b7cd5d22f32504202

Keywords: Bovine Seminal Ribonuclease, C-Terminal 3d Domain Swapping, Cytotoxic Rnase, Hinge Peptide, Multiple Swapping, Dimer, Isoenzyme, Amino Acid Sequence, Article, Carboxy Terminal Sequence, Chemical Model, Controlled Study, Enzyme Stability, Enzyme Structure, Mutation, Nonhuman, Priority Journal, Protein Function, Protein Quaternary Structure, Seminal Plasma, X Ray, Artificial Dimer Of Bs-Rnase Obtained By Incubation In Acetic Acid Of Mbs And Lyophilisation, Artificial Dimer Of Staa-Bs-Rnase Obtained By Incubation In Acetic Acid Of Staa-Mbs And Lyophilisation, Bovine Pancreatic Ribonuclease (ec 3 1 2 27 5), Covalent Swapped Isomer Of Bs-Rnase, Covalent Unswapped Isomer Of Bs-Rnase, D(art)-Bs, D(art)-Staa-Bs, Dithiothreitol, G16s N17t P19a S20a Variant Of Bs-Rnase, G16s N17t P19a S20a Variant Of Mbs, Iodoacetamide, L28q Variant Of Mbs, L28q-Mbs, M×m, Monomeric Derivative Of Bs-Rnase With Cysteines 31 And 32 Either Linked To Glutathione Moieties Or Alkylated With Iodoacetamide, Ncd-Bs, Non-Covalent Swapped Dimer Of Bs-Rnase With Cysteines 31 And 32 Linked To Iodoacetamide, Obtained By Selective Reduction Of The Swapped Isoform And Iodoalkylation, P19a L28q Variant Of Bs-Rnase, P19a L28q Variant Of Mbs, Palq-Bs-Rnase, Palq-Mbs, R80s Variant Of Staa-Bs-Rnase, R80s Variant Of Staa-Mbs, R80s-Staa-Bs-Rnase, R80s-Staa-Mbs, Ribonuclease Inhibitor, Size-Exclusion Chromatography, Animals, Cattle, Crystallography, X-Ray, Endoribonucleases, Molecular Sequence Data, Protein Multimerization, Protein Structure, Tertiary, D (art)-Bs, D (art)-Staa-Bs,

Affiliations:
*** IBB - CNR ***

Department of Chemical Sciences, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
National Institute Biostructures and Biosystems, Inter-University Consortium, Viale Medaglie d'Oro 305, I-00136 Rome, Italy


References:
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The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer

Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-terminal. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed. Structure summary of protein interactions: BS-RNase and BS-RNase bind by x-ray crystallography (View interaction) BS-RNase and BS-RNase bind by molecular sieving (1, 2) BS-RNase and BS-RNase bind by blue native page (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer

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The multiple forms of bovine seminal ribonuclease: Structure and stability of a C-terminal swapped dimer

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D'Errico G, Ercole C, Lista M, Pizzo E, Falanga A, Galdiero S, Spadaccini R, Picone D
* Enforcing the positive charge of N-termini enhances membrane interaction and antitumor activity of bovine seminal ribonuclease (813 views)
Bba-Gen Subjects (ISSN: 0005-2736, 0006-3002, 0925-4439), 2011 Dec; 1808(12): 3007-3015.
Impact Factor: 3.99
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Merlino A, Russo Krauss I, Perillo M, Mattia CA, Ercole C, Picone D, Vergara A, Sica F
* Toward an Antitumor Form of Bovine Pancreatic Ribonuclease: The Crystal Structure of Three Noncovalent Dimeric Mutants (498 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1029-1037.
Impact Factor: 2.605
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Merlino A, Ercole C, Picone D, Pizzo E, Mazzarella L, Sica F
* The buried diversity of bovine seminal ribonuclease: Shape and cytotoxicity of the swapped non-covalent form of the enzyme (742 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2008 Feb 15; 376(2): 427-437.
Impact Factor: 4.146
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Naddeo M, Vitagliano L, Russo A, Gotte G, D'Alessio G, Sorrentino S
* Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor (467 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 May 9; 579(12): 2663-2668.
Impact Factor: 3.415
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Picone D, Di Fiore A, Ercole C, Franzese M, Sica F, Tomaselli S, Mazzarella L
* The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (579 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Impact Factor: 5.854
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Sica F, Di Fiore A, Merlino A, Mazzarella L
* Structure and stability of the non-covalent swapped dimer of bovine seminal ribonuclease - An enzyme tailored to evade ribonuclease protein inhibitor (584 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2004 Sep 27; 279(35): 36753-36760.
Impact Factor: 6.355
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Merlino A, Vitagliano L, Sica F, Zagari A, Mazzarella L
* Population shift vs induced fit: The case of bovine seminal ribonuclease swapping dimer (437 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 689-695.
Impact Factor: 2.863
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Berisio R, Sica F, De Lorenzo C, Di Fiore A, Piccoli R, Zagari A, Mazzarella L
* Crystal Structure Of The Dimeric Un-Swapped Form Of Bovine Seminal Ribonuclease (445 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2003 Nov 6; 554(1-2): 105-110.
Impact Factor: 3.609
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Sica F, Di Fiore A, Zagari A, Mazzarella L
* The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative (420 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2003 Sep 1; 52(2): 263-271.
Impact Factor: 4.313
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Spalletti-cernia D, Sorrentino R, Di Gaetano S, Arciello A, Garbi C, Piccoli R, D'Alessio G, Vecchio G, Laccetti P, Santoro M
* Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis (465 views)
Journal Of Clinical Endocrinology & Metabolism (ISSN: 0021-972x), 2003 Jun; 88(6): 2900-2907.
Impact Factor: 5.873
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Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease (537 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 29; 293(3): 569-577.
Impact Factor: 5.501
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Sica F, Adinolfi S, Berisio R, De Lorenzo C, Mazzarella L, Piccoli R, Vitagliano L, Zagari A
Crystallization of multiple forms of bovine seminal ribonuclease in the liganded and unliganded state (369 views)
J Cryst Growth (ISSN: 0022-0248), 1999; 196(2-4): 305-312.
Impact Factor: 1.492
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Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine (564 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
Impact Factor: 4.44
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Sica F, Adinolfi S, Vitagliano L, Zagari A, Capasso S, Mazzarella L
Cosolute effect on crystallization of two dinucleotide complexes of bovine seminal ribonuclease from concentrated salt solutions (330 views)
J Cryst Growth (ISSN: 0022-0248), 1996; 168(1-4): 192-197.
Impact Factor: 1.259
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14 Records (14 excluding Abstracts).
Total impact factor: 55.715 (55.715 excluding Abstracts).
Total 5 year impact factor: 46.597 (46.597 excluding Abstracts).

Last modified by Marco Comerci on Sunday 12 July 2020, 13:14:52
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