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Article: Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk

TitleSolution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk
Authors
Issue Date2010
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2010, v. 38 n. 15, p. 5206-5216 How to Cite?
AbstractThe lateral stalk of ribosome is responsible for kingdom-specific binding of translation factors and activation of GTP hydrolysis that drives protein synthesis. In eukaryotes, the stalk is composed of acidic ribosomal proteins P0, P1 and P2 that constitute a pentameric P-complex in 1: 2: 2 ratio. We have determined the solution structure of the N-terminal dimerization domain of human P2 (NTD-P2), which provides insights into the structural organization of the eukaryotic stalk. Our structure revealed that eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. The two subunits of NTD-P2 form extensive hydrophobic interactions in the dimeric interface that buries 2400 Å 2 of solvent accessible surface area. We have showed that P1 can dissociate P2 homodimer spontaneously to form a more stable P1/P2 1: 1 heterodimer. By homology modelling, we identified three exposed polar residues on helix-3 of P2 are substituted by conserved hydrophobic residues in P1. Confirmed by mutagenesis, we showed that these residues on helix-3 of P1 are not involved in the dimerization of P1/P2, but instead play a vital role in anchoring P1/P2 heterodimer to P0. Based on our results, models of the eukaryotic stalk complex were proposed. © The Author(s) 2010. Published by Oxford University Press.
Persistent Identifierhttp://hdl.handle.net/10722/133605
ISSN
2015 Impact Factor: 9.202
2015 SCImago Journal Rankings: 7.458
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
NIHP41 RR-01081
Research Grants Council of Hong Kong SAR430103
477509
Chinese University of Hong Kong
Funding Information:

Molecular graphics images in Figure 6 and Supplementary Figure S4 were produced using the UCSF Chimera package from the Resource for Biocomputing, Visualization and Informatics at the University of California, San Francisco (supported by NIH P41 RR-01081). Other molecular images were produced by PyMOL.

References

 

DC FieldValueLanguage
dc.contributor.authorLee, KMen_HK
dc.contributor.authorYu, CWHen_HK
dc.contributor.authorChan, DSBen_HK
dc.contributor.authorChiu, TYHen_HK
dc.contributor.authorZhu, Gen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorShaw, PCen_HK
dc.contributor.authorWong, KBen_HK
dc.date.accessioned2011-05-24T02:11:38Z-
dc.date.available2011-05-24T02:11:38Z-
dc.date.issued2010en_HK
dc.identifier.citationNucleic Acids Research, 2010, v. 38 n. 15, p. 5206-5216en_HK
dc.identifier.issn0305-1048en_HK
dc.identifier.urihttp://hdl.handle.net/10722/133605-
dc.description.abstractThe lateral stalk of ribosome is responsible for kingdom-specific binding of translation factors and activation of GTP hydrolysis that drives protein synthesis. In eukaryotes, the stalk is composed of acidic ribosomal proteins P0, P1 and P2 that constitute a pentameric P-complex in 1: 2: 2 ratio. We have determined the solution structure of the N-terminal dimerization domain of human P2 (NTD-P2), which provides insights into the structural organization of the eukaryotic stalk. Our structure revealed that eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. The two subunits of NTD-P2 form extensive hydrophobic interactions in the dimeric interface that buries 2400 Å 2 of solvent accessible surface area. We have showed that P1 can dissociate P2 homodimer spontaneously to form a more stable P1/P2 1: 1 heterodimer. By homology modelling, we identified three exposed polar residues on helix-3 of P2 are substituted by conserved hydrophobic residues in P1. Confirmed by mutagenesis, we showed that these residues on helix-3 of P1 are not involved in the dimerization of P1/P2, but instead play a vital role in anchoring P1/P2 heterodimer to P0. Based on our results, models of the eukaryotic stalk complex were proposed. © The Author(s) 2010. Published by Oxford University Press.en_HK
dc.languageengen_US
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.rightsPre-print: Journal Title] ©: [year] [owner as specified on the article] Published by Oxford University Press [on behalf of xxxxxx]. All rights reserved. Pre-print (Once an article is published, preprint notice should be amended to): This is an electronic version of an article published in [include the complete citation information for the final version of the Article as published in the print edition of the Journal.] Post-print: This is a pre-copy-editing, author-produced PDF of an article accepted for publication in [insert journal title] following peer review. The definitive publisher-authenticated version [insert complete citation information here] is available online at: xxxxxxx [insert URL that the author will receive upon publication here].-
dc.subject.meshAmino Acid Sequence-
dc.subject.meshDimerization-
dc.subject.meshModels, Molecular-
dc.subject.meshPhosphoproteins - chemistry-
dc.subject.meshRibosomal Proteins - chemistry-
dc.titleSolution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalken_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0305-1048&volume=38&issue=15&spage=5206&epage=5216&date=2010&atitle=Solution+structure+of+the+dimerization+domain+of+ribosomal+protein+p2+provides+insights+for+the+structural+organization+of+eukaryotic+stalk-
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1093/nar/gkq231en_HK
dc.identifier.pmid20385603-
dc.identifier.pmcidPMC2926600-
dc.identifier.scopuseid_2-s2.0-77956123000en_HK
dc.identifier.hkuros185368en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77956123000&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume38en_HK
dc.identifier.issue15en_HK
dc.identifier.spage5206en_HK
dc.identifier.epage5216en_HK
dc.identifier.isiWOS:000281345900033-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLee, KM=8311540800en_HK
dc.identifier.scopusauthoridYu, CWH=36674170000en_HK
dc.identifier.scopusauthoridChan, DSB=16229503900en_HK
dc.identifier.scopusauthoridChiu, TYH=36730424600en_HK
dc.identifier.scopusauthoridZhu, G=7402633110en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridShaw, PC=35599523600en_HK
dc.identifier.scopusauthoridWong, KB=7404759301en_HK
dc.identifier.citeulike7028668-

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