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Article: Involvement of the amino-terminal β-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity

TitleInvolvement of the amino-terminal β-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity
Authors
Issue Date2001
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.org
Citation
Protein Science, 2001, v. 10 n. 8, p. 1658-1668 How to Cite?
AbstractRibotoxins are a family of potent cytotoxic proteins from Aspergillus whose members display a high sequence identity (85% for about 150 amino acid residues). The three-dimensional structures of two of these proteins, α-sarcin and restrictocin, are known. They interact with phospholipid bilayers, according to their ability to enter cells, and cleave a specific phosphodiester bond in the large subunit of ribosome thus inhibiting protein biosynthesis. Two nonconservative sequence changes between these proteins are located at the amino-terminal β-hairpin of α-sarcin, a characteristic structure that is absent in other nontoxic structurally related microbial RNases. These two residues of α-sarcin, Lys 11 and Thr 20, have been substituted with the equivalent amino acids in restrictocin. The single mutants (K11L and T20D) and the corresponding K11L/T20D double mutant have been produced in Escherichia coli and purified to homogeneity. The spectroscopic characterization of the purified proteins reveals that the overall native structure is preserved. The ribonuclease and lipid-perturbing activities of the three mutants and restrictocin have been evaluated and compared with those of α-sarcin. These proteins exhibit the same ability to specifically inactivate ribosomes, although they show different activity against nonspecific substrate analogs such as poly(A). The mutant variant K11L and restrictocin display a lower phospholipid-interacting ability correlated with a decreased cytotoxicity. The results obtained are interpreted in terms of the involvement of the amino-terminal β-hairpin in the interaction with both membranes and polyadenylic acid.
Persistent Identifierhttp://hdl.handle.net/10722/157324
ISSN
2015 Impact Factor: 3.039
2015 SCImago Journal Rankings: 2.029
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorGarcíaOrtega, Len_US
dc.contributor.authorLacadena, Jen_US
dc.contributor.authorMancheño, JMen_US
dc.contributor.authorOñaderra, Men_US
dc.contributor.authorKao, Ren_US
dc.contributor.authorDavies, Jen_US
dc.contributor.authorOlmo, Nen_US
dc.contributor.authorMartínez Del Pozo, Aen_US
dc.contributor.authorGavilanes, JGen_US
dc.date.accessioned2012-08-08T08:48:56Z-
dc.date.available2012-08-08T08:48:56Z-
dc.date.issued2001en_US
dc.identifier.citationProtein Science, 2001, v. 10 n. 8, p. 1658-1668en_US
dc.identifier.issn0961-8368en_US
dc.identifier.urihttp://hdl.handle.net/10722/157324-
dc.description.abstractRibotoxins are a family of potent cytotoxic proteins from Aspergillus whose members display a high sequence identity (85% for about 150 amino acid residues). The three-dimensional structures of two of these proteins, α-sarcin and restrictocin, are known. They interact with phospholipid bilayers, according to their ability to enter cells, and cleave a specific phosphodiester bond in the large subunit of ribosome thus inhibiting protein biosynthesis. Two nonconservative sequence changes between these proteins are located at the amino-terminal β-hairpin of α-sarcin, a characteristic structure that is absent in other nontoxic structurally related microbial RNases. These two residues of α-sarcin, Lys 11 and Thr 20, have been substituted with the equivalent amino acids in restrictocin. The single mutants (K11L and T20D) and the corresponding K11L/T20D double mutant have been produced in Escherichia coli and purified to homogeneity. The spectroscopic characterization of the purified proteins reveals that the overall native structure is preserved. The ribonuclease and lipid-perturbing activities of the three mutants and restrictocin have been evaluated and compared with those of α-sarcin. These proteins exhibit the same ability to specifically inactivate ribosomes, although they show different activity against nonspecific substrate analogs such as poly(A). The mutant variant K11L and restrictocin display a lower phospholipid-interacting ability correlated with a decreased cytotoxicity. The results obtained are interpreted in terms of the involvement of the amino-terminal β-hairpin in the interaction with both membranes and polyadenylic acid.en_US
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.proteinscience.orgen_US
dc.relation.ispartofProtein Scienceen_US
dc.subject.meshAllergensen_US
dc.subject.meshAmino Acid Substitutionen_US
dc.subject.meshAntigens, Planten_US
dc.subject.meshAspergillus - Chemistry - Genetics - Metabolismen_US
dc.subject.meshCytotoxins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshEndoribonucleases - Chemistry - Genetics - Metabolism - Toxicityen_US
dc.subject.meshEscherichia Coli - Geneticsen_US
dc.subject.meshFungal Proteins - Chemistry - Genetics - Metabolism - Toxicityen_US
dc.subject.meshHumansen_US
dc.subject.meshLipid Bilayers - Chemistry - Metabolismen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshMycotoxins - Chemistry - Genetics - Metabolism - Toxicityen_US
dc.subject.meshProtein Denaturationen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshProtein Synthesis Inhibitors - Chemistry - Metabolismen_US
dc.subject.meshRibonucleases - Chemistry - Genetics - Metabolism - Toxicityen_US
dc.subject.meshRibosomes - Metabolismen_US
dc.subject.meshSpectrometry, Fluorescenceen_US
dc.subject.meshTemperatureen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.titleInvolvement of the amino-terminal β-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activityen_US
dc.typeArticleen_US
dc.identifier.emailKao, R:rytkao@hkucc.hku.hken_US
dc.identifier.authorityKao, R=rp00481en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1110/ps.9601en_US
dc.identifier.pmid11468362-
dc.identifier.scopuseid_2-s2.0-0034925094en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034925094&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume10en_US
dc.identifier.issue8en_US
dc.identifier.spage1658en_US
dc.identifier.epage1668en_US
dc.identifier.isiWOS:000169984100019-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridGarcíaOrtega, L=6507071173en_US
dc.identifier.scopusauthoridLacadena, J=36475099200en_US
dc.identifier.scopusauthoridMancheño, JM=6701425928en_US
dc.identifier.scopusauthoridOñaderra, M=7004188455en_US
dc.identifier.scopusauthoridKao, R=7101675499en_US
dc.identifier.scopusauthoridDavies, J=7404982789en_US
dc.identifier.scopusauthoridOlmo, N=6603898788en_US
dc.identifier.scopusauthoridMartínez Del Pozo, A=35601641400en_US
dc.identifier.scopusauthoridGavilanes, JG=7005888348en_US

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