Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana L - Molecular characterisation and comparative structural analysis of similar ATP/ADP translocators from plastids and Rickettsia prowazekii

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dc.contributor.authorMohlmann, T
dc.contributor.authorTjaden, J
dc.contributor.authorSchwoppe, C
dc.contributor.authorWinkler, HH
dc.contributor.authorKampfenkel, K
dc.contributor.authorNeuhaus, HE
dc.date.accessioned2021-12-23T16:14:24Z-
dc.date.available2021-12-23T16:14:24Z-
dc.date.issued1998
dc.identifier.issn00142956
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11054-
dc.description.abstractRecently, we sequenced a cDNA clone from Arabidopsis thaliana L. encoding an ATP/ADP transporter protein (AATP1) located in the plastid envelope membrane. The deduced amino acid sequence of AATP1 exhibits a high degree of similarity (>66%) to the ATP/ADP transporter from the obligate intracellular gram-negative bacterium Rickettsia prowazekii. Here we report a second plastidic ATP/ADP carrier from A. thaliana (AATP2). As deduced from the amino acid sequence, AATP2 exhibits 77.6% identity to AATP1 and 36% to the rickettsial protein. Hydropathy analysis indicates that all three translocators are highly hydrophobic membrane proteins, which exhibit marked similarities and differences. The AATP1 translocator lacks the sixth transmembrane domain that is present in AATP2 and the bacterial transporter in R. prowazekii. In contrast to AATP1 and the bacterial transport protein, only AATP2 exhibits a truncated C-terminal end. To compare the general biochemical properties of AATP2 with the known transport properties of AATP1 we cloned the entire AATP2 cDNA into plasmid pJT118, leading to the presence of an additional N-terminal histidine tag of 10 amino acids. For heterologous expression of His(10)-AATP2 we chose the Escherichia coli strain C43, which was reported recently to allow overproduction of eucaryotic membrane transport proteins. After transformation and subsequent induction by isopropylthio-2-D-galactopyranoside intact E. coli cells harbouring plasmid pJT118 showed import of radioactively labelled ATP and ADP. As deduced from a Lineweaver-Burk analysis His(10)-AATP2 exhibited apparent K-m values for ATP and ADP of 22 mu M and 20 mu M, respectively. Import of ADP into His(10)-AATP2-expressing E. coli cells occurred at a rate of 24 nmol.mg protein(-1).h(-1), which was about threefold faster than import of ATP These biochemical characteristics are similar to transport properties of the heterologously expressed His(10)-AATP1 protein.
dc.description.sponsorshipNATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R01AI015035] Funding Source: NIH RePORTER; NIAID NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [AI-15035] Funding Source: Medline
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofEUROPEAN JOURNAL OF BIOCHEMISTRY
dc.subjectADENYLATE TRANSLOCATOR
dc.subjectAMYLOPLASTS
dc.subjectArabidopsis thaliana
dc.subjectATP/ADP transporter
dc.subjectBiochemistry & Molecular Biology
dc.subjectESCHERICHIA-COLI
dc.subjectFATTY-ACID
dc.subjectMITOCHONDRIA
dc.subjectNUCLEOTIDE-SEQUENCE
dc.subjectPHOSPHATE TRANSLOCATOR
dc.subjectplastid
dc.subjectPROTEIN
dc.subjectRickettsia prowazekii
dc.subjectSPINACH-CHLOROPLASTS
dc.subjectSTARCH SYNTHESIS
dc.titleOccurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana L - Molecular characterisation and comparative structural analysis of similar ATP/ADP translocators from plastids and Rickettsia prowazekii
dc.typejournal article
dc.identifier.doi10.1046/j.1432-1327.1998.2520353.x
dc.identifier.isiISI:000072617700003
dc.description.volume252
dc.description.issue3
dc.description.startpage353
dc.description.endpage359
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationEur. J. Biochem.
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