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Conference Paper: Structural characterization of human ribosomal protein P2 by NMR spectroscopy

TitleStructural characterization of human ribosomal protein P2 by NMR spectroscopy
Authors
Issue Date2005
Citation
Croucher Foundation Advanced Study Institute: Advances in Protein Sciences, Biochemistry Department, The Chinese University of Hong Kong, Hong Kong, 15-17 December 2005, p. 29, abstract no. PO-13 How to Cite?
AbstractRibosome consists of rRNAs and ribosomal proteins. Among the ribosomal proteins, three acidic ribosomal proteins P0, P1 and P2, which form P-complex, are located at the lateral stalk of the ribosome. The P-complex consists of one P0, two P1 and two P2, but the protein-protein interactions among these five proteins are still controversial. On the functional point of view, it has been reported that these proteins interact with mRNAs, tRNAs and translation factors during the course of protein synthesis. To understand the structure-function relationship, P2 was overexpressed in E. coli and purified by four chromatographic steps including ion-exchange, hydrophobic interaction and gel filtration chromatography. P2 was labeled with C13 and/or N15 isotopes and NMR experiments were performed. By triple resonance experiments, we have obtained the backbone 1H, 13C, and 15N resonances of P2. Secondary chemical shift values suggested that P2 has an N-terminal domain with four helices, and an unstructured C-terminal tail. Pull-down assay suggested that the N-terminal domain of P2 is responsible for dimerization with P1 to form a heterodimer, or with P2 to form a homodimer. The C-terminal tail of P2 was found to interact with eukaryotic elongation factor 2 (eEF2), which is an important factor in protein elongation.
Persistent Identifierhttp://hdl.handle.net/10722/97692

 

DC FieldValueLanguage
dc.contributor.authorLee, KMen_HK
dc.contributor.authorChan, SBen_HK
dc.contributor.authorChu, LOen_HK
dc.contributor.authorZhu, Gen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorShaw, PCen_HK
dc.contributor.authorWong, KBen_HK
dc.date.accessioned2010-09-25T17:18:34Z-
dc.date.available2010-09-25T17:18:34Z-
dc.date.issued2005en_HK
dc.identifier.citationCroucher Foundation Advanced Study Institute: Advances in Protein Sciences, Biochemistry Department, The Chinese University of Hong Kong, Hong Kong, 15-17 December 2005, p. 29, abstract no. PO-13en_HK
dc.identifier.urihttp://hdl.handle.net/10722/97692-
dc.description.abstractRibosome consists of rRNAs and ribosomal proteins. Among the ribosomal proteins, three acidic ribosomal proteins P0, P1 and P2, which form P-complex, are located at the lateral stalk of the ribosome. The P-complex consists of one P0, two P1 and two P2, but the protein-protein interactions among these five proteins are still controversial. On the functional point of view, it has been reported that these proteins interact with mRNAs, tRNAs and translation factors during the course of protein synthesis. To understand the structure-function relationship, P2 was overexpressed in E. coli and purified by four chromatographic steps including ion-exchange, hydrophobic interaction and gel filtration chromatography. P2 was labeled with C13 and/or N15 isotopes and NMR experiments were performed. By triple resonance experiments, we have obtained the backbone 1H, 13C, and 15N resonances of P2. Secondary chemical shift values suggested that P2 has an N-terminal domain with four helices, and an unstructured C-terminal tail. Pull-down assay suggested that the N-terminal domain of P2 is responsible for dimerization with P1 to form a heterodimer, or with P2 to form a homodimer. The C-terminal tail of P2 was found to interact with eukaryotic elongation factor 2 (eEF2), which is an important factor in protein elongation.-
dc.languageengen_HK
dc.relation.ispartofCroucher Foundation Advanced Study Institute: Advances in Protein Sciences, Biochemistry Department, The Chinese University of Hong Kong, Hong Kong, 15-17 December 2005en_HK
dc.titleStructural characterization of human ribosomal protein P2 by NMR spectroscopyen_HK
dc.typeConference_Paperen_HK
dc.identifier.emailSze, KH: khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.identifier.hkuros122679en_HK
dc.identifier.spage29-
dc.identifier.epage29en_HK

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