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Article: Single amino acid substitutions affecting the specificity of the fungal ribotoxin mitogillin

TitleSingle amino acid substitutions affecting the specificity of the fungal ribotoxin mitogillin
Authors
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2000, v. 466 n. 1, p. 87-90 How to Cite?
AbstractMitogillin and related fungal ribotoxins are small basic ribonucleolytic proteins that inhibit protein synthesis by specifically hydrolyzing a single phosphodiester bond in the universally conserved α-sarcin/ricin loop (SRL) of large subunit ribosomal RNAs. It was previously shown that mitogillin is a natural derivative of a T1/U2-like ribonuclease with inserted domains that are involved in target selection and specificity. Site-directed mutagenesis was used to substitute single amino acids in the previously identified functional domains Ala1-Tyr24 (B1-L1-B2 domain) and Lys106-Lys113 (L4 region). Examination of the activities of the mutants in the digestion of polyinosinic acid (a ribonuclease substrate) and specific cleavage of the SRL shows that Asn7Ala and Lys111Gln substitutions lead to altered ribonuclease activity and diminished substrate specificity consistent with the proposed functions of these domains. Copyright (C) 2000 Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/157311
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKao, Ren_US
dc.contributor.authorDavies, Jen_US
dc.date.accessioned2012-08-08T08:48:50Z-
dc.date.available2012-08-08T08:48:50Z-
dc.date.issued2000en_US
dc.identifier.citationFebs Letters, 2000, v. 466 n. 1, p. 87-90en_US
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/10722/157311-
dc.description.abstractMitogillin and related fungal ribotoxins are small basic ribonucleolytic proteins that inhibit protein synthesis by specifically hydrolyzing a single phosphodiester bond in the universally conserved α-sarcin/ricin loop (SRL) of large subunit ribosomal RNAs. It was previously shown that mitogillin is a natural derivative of a T1/U2-like ribonuclease with inserted domains that are involved in target selection and specificity. Site-directed mutagenesis was used to substitute single amino acids in the previously identified functional domains Ala1-Tyr24 (B1-L1-B2 domain) and Lys106-Lys113 (L4 region). Examination of the activities of the mutants in the digestion of polyinosinic acid (a ribonuclease substrate) and specific cleavage of the SRL shows that Asn7Ala and Lys111Gln substitutions lead to altered ribonuclease activity and diminished substrate specificity consistent with the proposed functions of these domains. Copyright (C) 2000 Federation of European Biochemical Societies.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_US
dc.relation.ispartofFEBS Lettersen_US
dc.subject.meshAllergensen_US
dc.subject.meshAmino Acid Substitutionen_US
dc.subject.meshAntigens, Planten_US
dc.subject.meshEscherichia Coli - Geneticsen_US
dc.subject.meshFungal Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshMycotoxins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshRna, Fungal - Metabolismen_US
dc.subject.meshRna, Ribosomal - Metabolismen_US
dc.subject.meshRecombinant Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRibonucleases - Chemistry - Genetics - Metabolismen_US
dc.subject.meshSubstrate Specificityen_US
dc.titleSingle amino acid substitutions affecting the specificity of the fungal ribotoxin mitogillinen_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.doi10.1016/S0014-5793(99)01753-6en_US
dc.identifier.pmid10648818-
dc.identifier.scopuseid_2-s2.0-0033954555en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033954555&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume466en_US
dc.identifier.issue1en_US
dc.identifier.spage87en_US
dc.identifier.epage90en_US
dc.identifier.isiWOS:000085022000018-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridKao, R=7101675499en_US
dc.identifier.scopusauthoridDavies, J=7404982789en_US

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