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Article: Investigation into the interactions between diadenosine 5′,5‴-P1,P4-tetraphosphate and two proteins: Molecular chaperone GroEL and cAMP receptor protein

TitleInvestigation into the interactions between diadenosine 5′,5‴-P1,P4-tetraphosphate and two proteins: Molecular chaperone GroEL and cAMP receptor protein
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 2006, v. 45 n. 9, p. 3095-3106 How to Cite?
AbstractDiadenosine 5′,5‴-P1,P4-tetraphosphate (Ap4A) is a dinucleoside polyphosphate found ubiquitously in eukaryotic and prokaryotic cells. Despite Ap4A being universal, its functions have proved to be difficult to define, although they appear to have a strong presence during cellular stress. Here we report on our investigations into the nature and properties of putative Ap4A interactions with Escherichia coli molecular chaperone GroEL and cAMP receptor protein (CRP). We confirm previous literature observations that GroEL is an Ap4A binding protein and go on to prove that binding of Ap4A to GroEL involves a set of binding sites (one per monomer) distinct from the well-known GroEL ATP/ADP sites. Binding of Ap4A to GroEL appears to enhance ATPase rates at higher temperatures, encourages the release of bound ADP, and may promote substrate protein release through differential destabilization of the substrate protein-GroEL complex. We suggest that such effects should result in enhanced GroEL/GroES chaperoning activities that could be a primary reason for the improved yields of the refolded substrate protein observed during GroEL/GroES-assisted folding and refolding at ≥30 °C in the presence of Ap4A. In contrast, we were unable to obtain any data to support a direct role for Ap4A interactions with CRP. © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/147533
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTanner, JAen_US
dc.contributor.authorWright, Men_US
dc.contributor.authorChristie, EMen_US
dc.contributor.authorPreuss, MKen_US
dc.contributor.authorMiller, ADen_US
dc.date.accessioned2012-05-29T06:04:25Z-
dc.date.available2012-05-29T06:04:25Z-
dc.date.issued2006en_US
dc.identifier.citationBiochemistry, 2006, v. 45 n. 9, p. 3095-3106en_US
dc.identifier.issn0006-2960en_US
dc.identifier.urihttp://hdl.handle.net/10722/147533-
dc.description.abstractDiadenosine 5′,5‴-P1,P4-tetraphosphate (Ap4A) is a dinucleoside polyphosphate found ubiquitously in eukaryotic and prokaryotic cells. Despite Ap4A being universal, its functions have proved to be difficult to define, although they appear to have a strong presence during cellular stress. Here we report on our investigations into the nature and properties of putative Ap4A interactions with Escherichia coli molecular chaperone GroEL and cAMP receptor protein (CRP). We confirm previous literature observations that GroEL is an Ap4A binding protein and go on to prove that binding of Ap4A to GroEL involves a set of binding sites (one per monomer) distinct from the well-known GroEL ATP/ADP sites. Binding of Ap4A to GroEL appears to enhance ATPase rates at higher temperatures, encourages the release of bound ADP, and may promote substrate protein release through differential destabilization of the substrate protein-GroEL complex. We suggest that such effects should result in enhanced GroEL/GroES chaperoning activities that could be a primary reason for the improved yields of the refolded substrate protein observed during GroEL/GroES-assisted folding and refolding at ≥30 °C in the presence of Ap4A. In contrast, we were unable to obtain any data to support a direct role for Ap4A interactions with CRP. © 2006 American Chemical Society.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_US
dc.relation.ispartofBiochemistryen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshChaperonin 60 - Chemistry - Genetics - Metabolismen_US
dc.subject.meshCircular Dichroismen_US
dc.subject.meshCyclic Amp Receptor Protein - Chemistry - Genetics - Metabolismen_US
dc.subject.meshDinucleoside Phosphates - Genetics - Metabolismen_US
dc.subject.meshEscherichia Coli - Metabolismen_US
dc.subject.meshMolecular Chaperonesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshTemperatureen_US
dc.titleInvestigation into the interactions between diadenosine 5′,5‴-P1,P4-tetraphosphate and two proteins: Molecular chaperone GroEL and cAMP receptor proteinen_US
dc.typeArticleen_US
dc.identifier.emailTanner, JA:jatanner@hku.hken_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/bi052529ken_US
dc.identifier.pmid16503665-
dc.identifier.scopuseid_2-s2.0-33644694068en_US
dc.identifier.hkuros114587-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33644694068&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume45en_US
dc.identifier.issue9en_US
dc.identifier.spage3095en_US
dc.identifier.epage3106en_US
dc.identifier.isiWOS:000235792500036-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridTanner, JA=35513993000en_US
dc.identifier.scopusauthoridWright, M=11139776500en_US
dc.identifier.scopusauthoridChristie, EM=12765499000en_US
dc.identifier.scopusauthoridPreuss, MK=7006673640en_US
dc.identifier.scopusauthoridMiller, AD=7406230808en_US

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