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Article: Solution Structure of an Active Mutant of Maize Ribosome-Inactivating Protein (MOD) and Its Interaction with the Ribosomal Stalk Protein P2

TitleSolution Structure of an Active Mutant of Maize Ribosome-Inactivating Protein (MOD) and Its Interaction with the Ribosomal Stalk Protein P2
Authors
Issue Date2010
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2010, v. 395 n. 5, p. 897-907 How to Cite?
AbstractRibosome-inactivating proteins (RIPs) are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA. This modification renders the ribosome unable to bind the elongation factors, thereby inhibiting the protein synthesis. Maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein. In this study, we describe the first solution structure of this type of RIP, a  28-kDa active mutant of maize RIP (MOD). The overall protein structure of MOD is comparable to those of the other type I RIPs and the A-chain of type II RIPs but shows significant differences in specific regions, including (1) shorter β6 and αB segments, probably for accommodating easier substrate binding, and (2) an α-helix instead of an antiparallel β-sheet in the C-terminal domain, which has been reported to be involved in binding ribosomal protein P2 in some RIPs. Furthermore, NMR chemical shift perturbation experiments revealed that the P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region. This relocation of the P2 binding site can be rationalized by concerted changes in the electrostatic surface potential and 3D structures on the MOD protein and provides vital clues about the underlying molecular mechanism of this unique type of RIP. © 2009 Elsevier Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/157575
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
Funding AgencyGrant Number
Research Grant Council of Hong KongGRF 7533/06M
7755/08M
4606/06M
Funding Information:

This work was supported by grants from the Research Grant Council of Hong Kong (GRF 7533/06M and 7755/08M for K. H. Sze and 4606/06M for P.-C Shaw). We thank Prof. R.S. Boston of North Carolina State University for providing the clones of maize RIP

References

 

DC FieldValueLanguage
dc.contributor.authorYang, Yen_US
dc.contributor.authorMak, ANSen_US
dc.contributor.authorShaw, PCen_US
dc.contributor.authorSze, KHen_US
dc.date.accessioned2012-08-08T08:51:23Z-
dc.date.available2012-08-08T08:51:23Z-
dc.date.issued2010en_US
dc.identifier.citationJournal Of Molecular Biology, 2010, v. 395 n. 5, p. 897-907en_US
dc.identifier.issn0022-2836en_US
dc.identifier.urihttp://hdl.handle.net/10722/157575-
dc.description.abstractRibosome-inactivating proteins (RIPs) are N-glycosidases that depurinate a specific adenine residue in the conserved sarcin/ricin loop of ribosomal RNA. This modification renders the ribosome unable to bind the elongation factors, thereby inhibiting the protein synthesis. Maize RIP, a type III RIP, is unique compared to the other type I and type II RIPs because it is synthesized as a precursor with a 25-residue internal inactivation region, which is removed in order to activate the protein. In this study, we describe the first solution structure of this type of RIP, a  28-kDa active mutant of maize RIP (MOD). The overall protein structure of MOD is comparable to those of the other type I RIPs and the A-chain of type II RIPs but shows significant differences in specific regions, including (1) shorter β6 and αB segments, probably for accommodating easier substrate binding, and (2) an α-helix instead of an antiparallel β-sheet in the C-terminal domain, which has been reported to be involved in binding ribosomal protein P2 in some RIPs. Furthermore, NMR chemical shift perturbation experiments revealed that the P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region. This relocation of the P2 binding site can be rationalized by concerted changes in the electrostatic surface potential and 3D structures on the MOD protein and provides vital clues about the underlying molecular mechanism of this unique type of RIP. © 2009 Elsevier Ltd.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_US
dc.relation.ispartofJournal of Molecular Biologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutationen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshPhosphoproteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshPlant Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshProtein Interaction Domains And Motifsen_US
dc.subject.meshRecombinant Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRibosomal Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshRibosome Inactivating Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshStatic Electricityen_US
dc.subject.meshZea Mays - Chemistry - Genetics - Metabolismen_US
dc.titleSolution Structure of an Active Mutant of Maize Ribosome-Inactivating Protein (MOD) and Its Interaction with the Ribosomal Stalk Protein P2en_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.jmb.2009.10.051en_US
dc.identifier.pmid19900464-
dc.identifier.scopuseid_2-s2.0-73649148999en_US
dc.identifier.hkuros172736-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-73649148999&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume395en_US
dc.identifier.issue5en_US
dc.identifier.spage897en_US
dc.identifier.epage907en_US
dc.identifier.isiWOS:000274922400001-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridYang, Y=7409391816en_US
dc.identifier.scopusauthoridMak, ANS=36780323900en_US
dc.identifier.scopusauthoridShaw, PC=35599523600en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US

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