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Article: Single amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeats

TitleSingle amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeats
Authors
KeywordsAnkyrin repeats
In vitro mutagenesis
Lipid metabolism
Lipid transfer
Issue Date2000
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412
Citation
Plant Molecular Biology, 2000, v. 44 n. 6, p. 711-721 How to Cite?
AbstractCytosolic acyl-CoA-binding proteins (ACBPs) are small proteins (ca. 10 kDa) that bind long-chain acyl-CoAs and are involved in the storage and intracellular transport of acyl-CoAs. Previously, we have characterized an Arabidopsis thaliana cDNA encoding a novel membrane-associated ACBP, designated ACBP1, demonstrating the existence of a new form of ACBP in plants (M.-L. Chye. Plant Mol. Biol. 38 (1998) 827-838). ACBPI likely participates in intermembrane lipid transport from the ER to the plasma membrane, where it could maintain a membrane-associated acyl pool (Chye et al., Plant J. 18 (1999) 205-214). Here we report the isolation of cDNAs encoding ACBP2 (Mr 38 479) that shows conservation in the acyl-CoA-binding domain to previously reported ACBPs, and contains ankyrin repeats at its carboxy terminus. These repeats, which likely mediate protein-protein interactions, could constitute a potential docking site in ACBP2 for an enzyme that uses acyl-CoAs as substrate. In vitro binding assays on recombinant (His)6-ACBP2 expressed in Escherichia coli show that it binds 14[C]palmitoyl-CoA preferentially to 14[C]oleoyl-CoA. Analysis of the acyl-CoA-binding domain in ACBP2 was carried out by in vitro mutagenesis. Mutant forms of recombinant (His)6-ACBP2 with single amino acid substitutions at conserved residues within the acyl-CoA-binding domain were less effective in binding14[C]palmitoyl-CoA. Northern blot analysis showed that the 1.6 kb ACBP2 mRNA, like that of ACBP1, is expressed in all plant organs. Analysis of the ACBP2 promoter revealed that, like the ACBP1 promoter, it lacks a TATA box suggesting the possibility of a housekeeping function for ACBP2 in plant lipid metabolism.
Persistent Identifierhttp://hdl.handle.net/10722/68460
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 1.915
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChye, MLen_HK
dc.contributor.authorLi, HYen_HK
dc.contributor.authorYung, MHen_HK
dc.date.accessioned2010-09-06T06:04:48Z-
dc.date.available2010-09-06T06:04:48Z-
dc.date.issued2000en_HK
dc.identifier.citationPlant Molecular Biology, 2000, v. 44 n. 6, p. 711-721en_HK
dc.identifier.issn0167-4412en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68460-
dc.description.abstractCytosolic acyl-CoA-binding proteins (ACBPs) are small proteins (ca. 10 kDa) that bind long-chain acyl-CoAs and are involved in the storage and intracellular transport of acyl-CoAs. Previously, we have characterized an Arabidopsis thaliana cDNA encoding a novel membrane-associated ACBP, designated ACBP1, demonstrating the existence of a new form of ACBP in plants (M.-L. Chye. Plant Mol. Biol. 38 (1998) 827-838). ACBPI likely participates in intermembrane lipid transport from the ER to the plasma membrane, where it could maintain a membrane-associated acyl pool (Chye et al., Plant J. 18 (1999) 205-214). Here we report the isolation of cDNAs encoding ACBP2 (Mr 38 479) that shows conservation in the acyl-CoA-binding domain to previously reported ACBPs, and contains ankyrin repeats at its carboxy terminus. These repeats, which likely mediate protein-protein interactions, could constitute a potential docking site in ACBP2 for an enzyme that uses acyl-CoAs as substrate. In vitro binding assays on recombinant (His)6-ACBP2 expressed in Escherichia coli show that it binds 14[C]palmitoyl-CoA preferentially to 14[C]oleoyl-CoA. Analysis of the acyl-CoA-binding domain in ACBP2 was carried out by in vitro mutagenesis. Mutant forms of recombinant (His)6-ACBP2 with single amino acid substitutions at conserved residues within the acyl-CoA-binding domain were less effective in binding14[C]palmitoyl-CoA. Northern blot analysis showed that the 1.6 kb ACBP2 mRNA, like that of ACBP1, is expressed in all plant organs. Analysis of the ACBP2 promoter revealed that, like the ACBP1 promoter, it lacks a TATA box suggesting the possibility of a housekeeping function for ACBP2 in plant lipid metabolism.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0167-4412en_HK
dc.relation.ispartofPlant Molecular Biologyen_HK
dc.subjectAnkyrin repeatsen_HK
dc.subjectIn vitro mutagenesisen_HK
dc.subjectLipid metabolismen_HK
dc.subjectLipid transferen_HK
dc.titleSingle amino acid substitutions at the acyl-CoA-binding domain interrupt 14[C]palmitoyl-CoA binding of ACBP2, an Arabidopsis acyl-CoA-binding protein with ankyrin repeatsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0167-4412&volume=44&spage=711&epage=721&date=2000&atitle=Single+amino+acid+substitutions+at+the+acyl-CoA-binding+domain+interrupt+14[C]palmitoyl-CoA+binding+of+ACBP2,+an+Arabidopsis+acyl-CoA-binding+protein+with+ankyrin+repeatsen_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1023/A:1026524108095en_HK
dc.identifier.pmid11202434-
dc.identifier.scopuseid_2-s2.0-0034488568en_HK
dc.identifier.hkuros63000en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034488568&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume44en_HK
dc.identifier.issue6en_HK
dc.identifier.spage711en_HK
dc.identifier.epage721en_HK
dc.identifier.isiWOS:000165792000003-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK
dc.identifier.scopusauthoridLi, HY=22953303900en_HK
dc.identifier.scopusauthoridYung, MH=7101896815en_HK

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