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Article: Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins

TitlePost-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins
Authors
Issue Date1997
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 1997, v. 405 n. 3, p. 267-272 How to Cite?
AbstractExpression in Escherichia coli of Streptomgces acyl carrier proteins (ACPs) associated with polyketide biosynthesis using the pT7-7 expression system of Tabor and Richardson led to the production predominantly of inactive ape-proteins lacking the 4'-phosphopantetheinyl prosthetic group essential for polyketide synthase activity. Modification of growth conditions led to an increase of production of active holo-protein for the actinorhodin (act) ACP, but this technique was ineffective for oxytetracycline (otc) and griseusin (gris) ACPs. Labelling experiments revealed that a low level of otc ACP expressed prior to induction was produced mainly as active holo-protein, while post-induction 15N-labelled protein was almost exclusively in the apo-ACPP form. Limiting endogenous holo-acyl carrier protein synthase (ACPS) concentration was implicated as responsible for low apo-ACP to holo-ACP conversion, rather than limiting substrate (coenzyme A) and cofactor (Mg2+) concentrations. Co-expression of act and gris ACPs with ACPS in E. coli led to high levels of production of active holo-ACPs and ACPS. We have also made the significant observation that AGES is able to transfer acylated CoA moieties to act apo-ACP.
Persistent Identifierhttp://hdl.handle.net/10722/147418
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCox, RJen_US
dc.contributor.authorHitchman, TSen_US
dc.contributor.authorByrom, KJen_US
dc.contributor.authorFindlow, ISCen_US
dc.contributor.authorTanner, JAen_US
dc.contributor.authorCrosby, Jen_US
dc.contributor.authorSimpson, TJen_US
dc.date.accessioned2012-05-29T06:03:35Z-
dc.date.available2012-05-29T06:03:35Z-
dc.date.issued1997en_US
dc.identifier.citationFebs Letters, 1997, v. 405 n. 3, p. 267-272en_US
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/10722/147418-
dc.description.abstractExpression in Escherichia coli of Streptomgces acyl carrier proteins (ACPs) associated with polyketide biosynthesis using the pT7-7 expression system of Tabor and Richardson led to the production predominantly of inactive ape-proteins lacking the 4'-phosphopantetheinyl prosthetic group essential for polyketide synthase activity. Modification of growth conditions led to an increase of production of active holo-protein for the actinorhodin (act) ACP, but this technique was ineffective for oxytetracycline (otc) and griseusin (gris) ACPs. Labelling experiments revealed that a low level of otc ACP expressed prior to induction was produced mainly as active holo-protein, while post-induction 15N-labelled protein was almost exclusively in the apo-ACPP form. Limiting endogenous holo-acyl carrier protein synthase (ACPS) concentration was implicated as responsible for low apo-ACP to holo-ACP conversion, rather than limiting substrate (coenzyme A) and cofactor (Mg2+) concentrations. Co-expression of act and gris ACPs with ACPS in E. coli led to high levels of production of active holo-ACPs and ACPS. We have also made the significant observation that AGES is able to transfer acylated CoA moieties to act apo-ACP.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_US
dc.relation.ispartofFEBS Lettersen_US
dc.subject.meshAcyl Carrier Protein - Metabolismen_US
dc.subject.meshApoproteins - Metabolismen_US
dc.subject.meshCoenzyme A - Metabolismen_US
dc.subject.meshDisulfidesen_US
dc.subject.meshEscherichia Coli - Enzymologyen_US
dc.subject.meshMultienzyme Complexes - Metabolismen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshRecombinant Proteinsen_US
dc.subject.meshSpecies Specificityen_US
dc.subject.meshStreptomyces - Enzymologyen_US
dc.titlePost-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteinsen_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.doi10.1016/S0014-5793(97)00202-0en_US
dc.identifier.pmid9108302-
dc.identifier.scopuseid_2-s2.0-0030936596en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030936596&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume405en_US
dc.identifier.issue3en_US
dc.identifier.spage267en_US
dc.identifier.epage272en_US
dc.identifier.isiWOS:A1997WT21700005-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridCox, RJ=7403420504en_US
dc.identifier.scopusauthoridHitchman, TS=6507393048en_US
dc.identifier.scopusauthoridByrom, KJ=7801496931en_US
dc.identifier.scopusauthoridFindlow, ISC=12786975800en_US
dc.identifier.scopusauthoridTanner, JA=35513993000en_US
dc.identifier.scopusauthoridCrosby, J=7103258887en_US
dc.identifier.scopusauthoridSimpson, TJ=7202539073en_US

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