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Article: Molecular dissection of mitogillin reveals that the fungal ribotoxins are a family of natural genetically engineered ribonucleases

TitleMolecular dissection of mitogillin reveals that the fungal ribotoxins are a family of natural genetically engineered ribonucleases
Authors
Issue Date1999
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1999, v. 274 n. 18, p. 12576-12582 How to Cite?
AbstractMitogillin and the related fungal ribotoxins are highly specific ribonucleases which inactivate the ribosome enzymatically by cleaving the 23- 28 S RNA of the large ribosomal subunit at a single phosphodiester bond. The site of cleavage occurs between G4325 and A4326 (rat ribosome numbering) which are present in one of the most conserved sequences (the α- sarcin loop) among the large subunit ribosomal RNAs of all living species. Amino acid sequence comparison of ribotoxins and guanyl/purine ribonucleases have identified domains or residues likely involved in ribonucleolytic activity or cleavage specificity. Fifteen deletion mutants (each 4 to 8 amino acid deletions) in motifs of mitogillin showing little amino acid sequence homology with guanyl/purine ribonucleases were constructed by site-directed mutagenesis. Analyses of the purified mutant proteins identified those regions in fungal ribotoxins contributing to ribosome targeting and modulating the catalytic activity of the toxin; some of the identified motifs are homologous to sequences in ribosomal proteins and elongation factors. This mutational study of mitogillin together with the recently published x- ray structure of restrictocin (a close relative of mitogillin) supports the hypothesis that the specific cleavage properties of ribotoxins are the result of natural genetic engineering in which the ribosomal targeting elements of ribosome-associated proteins were inserted into nonessential regions of T1- like ribonucleases.
Persistent Identifierhttp://hdl.handle.net/10722/157306
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKao, Ren_US
dc.contributor.authorDavies, Jen_US
dc.date.accessioned2012-08-08T08:48:48Z-
dc.date.available2012-08-08T08:48:48Z-
dc.date.issued1999en_US
dc.identifier.citationJournal Of Biological Chemistry, 1999, v. 274 n. 18, p. 12576-12582en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/157306-
dc.description.abstractMitogillin and the related fungal ribotoxins are highly specific ribonucleases which inactivate the ribosome enzymatically by cleaving the 23- 28 S RNA of the large ribosomal subunit at a single phosphodiester bond. The site of cleavage occurs between G4325 and A4326 (rat ribosome numbering) which are present in one of the most conserved sequences (the α- sarcin loop) among the large subunit ribosomal RNAs of all living species. Amino acid sequence comparison of ribotoxins and guanyl/purine ribonucleases have identified domains or residues likely involved in ribonucleolytic activity or cleavage specificity. Fifteen deletion mutants (each 4 to 8 amino acid deletions) in motifs of mitogillin showing little amino acid sequence homology with guanyl/purine ribonucleases were constructed by site-directed mutagenesis. Analyses of the purified mutant proteins identified those regions in fungal ribotoxins contributing to ribosome targeting and modulating the catalytic activity of the toxin; some of the identified motifs are homologous to sequences in ribosomal proteins and elongation factors. This mutational study of mitogillin together with the recently published x- ray structure of restrictocin (a close relative of mitogillin) supports the hypothesis that the specific cleavage properties of ribotoxins are the result of natural genetic engineering in which the ribosomal targeting elements of ribosome-associated proteins were inserted into nonessential regions of T1- like ribonucleases.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAllergensen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAntigens, Planten_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshFungal Proteins - Chemistry - Geneticsen_US
dc.subject.meshHydrogen Bondingen_US
dc.subject.meshHydrolysisen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshMycotoxins - Chemistry - Geneticsen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshRibonucleases - Chemistry - Geneticsen_US
dc.titleMolecular dissection of mitogillin reveals that the fungal ribotoxins are a family of natural genetically engineered ribonucleasesen_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.doi10.1074/jbc.274.18.12576en_US
dc.identifier.pmid10212236en_US
dc.identifier.scopuseid_2-s2.0-0033617455en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033617455&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume274en_US
dc.identifier.issue18en_US
dc.identifier.spage12576en_US
dc.identifier.epage12582en_US
dc.identifier.isiWOS:000080056800056-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKao, R=7101675499en_US
dc.identifier.scopusauthoridDavies, J=7404982789en_US

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