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Article: Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses

TitleInteraction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses
Authors
Issue Date2007
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2007, v. 35 n. 5, p. 1660-1672 How to Cite?
AbstractTrichosanthin (TCS) is a type I ribosome-inactivating protein that inactivates ribosome by enzymatically depurinating the A 4324 at the α-sarcin/ricin loop of 28S rRNA. We have shown in this and previous studies that TCS interacts with human acidic ribosomal proteins P0, P1 and P2, which constitute the lateral stalk of eukaryotic ribosome. Deletion mutagenesis showed that TCS interacts with the C-terminal tail of P2, the sequences of which are conserved in P0, P1 and P2. The P2-binding site on TCS was mapped to the C-terminal domain by chemical shift perturbation experiments. Scanning charge-to-alanine mutagenesis has shown that K173, R174 and K177 in the C-terminal domain of TCS are involved in interacting with the P2, presumably through forming charge-charge interactions to the conserved DDD motif at the C-terminal tail of P2. A triple-alanine variant K173A/R174A/K177A of TCS, which fails to bind P2 and ribosomal stalk in vitro, was found to be 18-fold less active in inhibiting translation in rabbit reticulocyte lysate, suggesting that interaction with P-proteins is required for full activity of TCS. In an analogy to the role of stalk proteins in binding elongation factors, we propose that interaction with acidic ribosomal stalk proteins help TCS to locate its RNA substrate. © 2007 Oxford University Press.
Persistent Identifierhttp://hdl.handle.net/10722/70456
ISSN
2015 Impact Factor: 9.202
2015 SCImago Journal Rankings: 7.458
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, DSBen_HK
dc.contributor.authorChu, LOen_HK
dc.contributor.authorLee, KMen_HK
dc.contributor.authorToo, PHMen_HK
dc.contributor.authorMa, KWen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorZhu, Gen_HK
dc.contributor.authorShaw, PCen_HK
dc.contributor.authorWong, KBen_HK
dc.date.accessioned2010-09-06T06:23:03Z-
dc.date.available2010-09-06T06:23:03Z-
dc.date.issued2007en_HK
dc.identifier.citationNucleic Acids Research, 2007, v. 35 n. 5, p. 1660-1672en_HK
dc.identifier.issn0305-1048en_HK
dc.identifier.urihttp://hdl.handle.net/10722/70456-
dc.description.abstractTrichosanthin (TCS) is a type I ribosome-inactivating protein that inactivates ribosome by enzymatically depurinating the A 4324 at the α-sarcin/ricin loop of 28S rRNA. We have shown in this and previous studies that TCS interacts with human acidic ribosomal proteins P0, P1 and P2, which constitute the lateral stalk of eukaryotic ribosome. Deletion mutagenesis showed that TCS interacts with the C-terminal tail of P2, the sequences of which are conserved in P0, P1 and P2. The P2-binding site on TCS was mapped to the C-terminal domain by chemical shift perturbation experiments. Scanning charge-to-alanine mutagenesis has shown that K173, R174 and K177 in the C-terminal domain of TCS are involved in interacting with the P2, presumably through forming charge-charge interactions to the conserved DDD motif at the C-terminal tail of P2. A triple-alanine variant K173A/R174A/K177A of TCS, which fails to bind P2 and ribosomal stalk in vitro, was found to be 18-fold less active in inhibiting translation in rabbit reticulocyte lysate, suggesting that interaction with P-proteins is required for full activity of TCS. In an analogy to the role of stalk proteins in binding elongation factors, we propose that interaction with acidic ribosomal stalk proteins help TCS to locate its RNA substrate. © 2007 Oxford University Press.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/en_HK
dc.relation.ispartofNucleic Acids Researchen_HK
dc.rightsNucleic Acids Research . Copyright © Oxford University Press.en_HK
dc.subject.meshAlanine - geneticsen_HK
dc.subject.meshAmino Acid Motifsen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAmino Acid Substitutionen_HK
dc.subject.meshBinding Sitesen_HK
dc.subject.meshConserved Sequenceen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMutagenesisen_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshPhosphoproteins - chemistry - genetics - metabolismen_HK
dc.subject.meshProtein Biosynthesis - drug effectsen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshRibosomal Proteins - chemistry - genetics - metabolismen_HK
dc.subject.meshSequence Deletionen_HK
dc.subject.meshTrichosanthin - chemistry - genetics - pharmacologyen_HK
dc.titleInteraction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analysesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0305-1048&volume=35&spage=1660&epage=1672&date=2007&atitle=Interaction+Between+Trichosanthin,+a+Ribosome-Inactivating+Protein,+and+the+Ribosomal+Stalk+Protein+P2+by+Chemical+Shift+Perturbation+and+Mutagenesis+Analyses+en_HK
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1093/nar/gkm065en_HK
dc.identifier.pmid17308345-
dc.identifier.scopuseid_2-s2.0-34247135324en_HK
dc.identifier.hkuros132726en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34247135324&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume35en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1660en_HK
dc.identifier.epage1672en_HK
dc.identifier.isiWOS:000246371200025-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridChan, DSB=16229503900en_HK
dc.identifier.scopusauthoridChu, LO=16229353000en_HK
dc.identifier.scopusauthoridLee, KM=8311540800en_HK
dc.identifier.scopusauthoridToo, PHM=36948012800en_HK
dc.identifier.scopusauthoridMa, KW=14828060700en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridZhu, G=7402633110en_HK
dc.identifier.scopusauthoridShaw, PC=35599523600en_HK
dc.identifier.scopusauthoridWong, KB=7404759301en_HK
dc.identifier.citeulike1235538-

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