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Titolo:
OCCURRENCE OF 2 PLASTIDIC ATP ADP TRANSPORTERS IN ARABIDOPSIS-THALIANA L - MOLECULAR CHARACTERIZATION AND COMPARATIVE STRUCTURAL-ANALYSIS OF SIMILAR ATP/ADP TRANSLOCATORS FROM PLASTIDS AND RICKETTSIA-PROWAZEKII/
Autore:
MOHLMANN T; TJADEN J; SCHWOPPE C; WINKLER HH; KAMPFENKEL K; NEUHAUS HE;
Indirizzi:
UNIV OSNABRUCK,BARBARASTR 11 D-49069 OSNABRUCK GERMANY UNIV OSNABRUCK D-49069 OSNABRUCK GERMANY UNIV S ALABAMA,COLL MED,MOL BIOL LAB,DEPT MICROBIOL & IMMUNOL MOBILE AL 00000 HOECHST MARION ROUSSEL FRANKFURT GERMANY
Titolo Testata:
European journal of biochemistry
fascicolo: 3, volume: 252, anno: 1998,
pagine: 353 - 359
SICI:
0014-2956(1998)252:3<353:OO2PAA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHATE TRANSLOCATOR; NUCLEOTIDE-SEQUENCE; STARCH SYNTHESIS; ADENYLATE TRANSLOCATOR; SPINACH-CHLOROPLASTS; ESCHERICHIA-COLI; FATTY-ACID; PROTEIN; MITOCHONDRIA; AMYLOPLASTS;
Keywords:
ARABIDOPSIS THALIANA; RICKETTSIA PROWAZEKII; ATP/ADP TRANSPORTER; PLASTID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
T. Mohlmann et al., "OCCURRENCE OF 2 PLASTIDIC ATP ADP TRANSPORTERS IN ARABIDOPSIS-THALIANA L - MOLECULAR CHARACTERIZATION AND COMPARATIVE STRUCTURAL-ANALYSIS OF SIMILAR ATP/ADP TRANSLOCATORS FROM PLASTIDS AND RICKETTSIA-PROWAZEKII/", European journal of biochemistry, 252(3), 1998, pp. 353-359

Abstract

Recently, 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 AATP1translocator 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 entireAATP2 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, whichwas 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 apparentK-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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:39:01