Identification of the human mitochondrial S-adenosylmethionine transporter:: bacterial expression, reconstitution, functional characterization and tissue distribution

被引:127
|
作者
Agrimi, G
Di Noia, MA
Marobbio, CMT
Fiermonte, G
Lasorsa, FM
Palmieri, F
机构
[1] Univ Bari, Dept Pharmacobiol, Biochem & Mol Biol Lab, I-70125 Bari, Italy
[2] CNR, Inst Biomembranes & Bioenerget, I-70125 Bari, Italy
关键词
mitochondria; mitochondrial carrier; proteomics; S-adenosylmethionine carrier; transport;
D O I
10.1042/BJ20031664
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mitochondrial carriers are a family of transport proteins that with a few exceptions. are found in the inner membranes of mitochondria. They shuttle metabolites and cofactors through this membrane. and connect cytoplasmic functions with others in the matrix. SAM (S-adenosylinethionine) hits to be transported into the mitochondria w,here it is converted into S-adenosylhomocysteine in methylation reactions of DNA, RNA and proteins. The transport of SAM has been investigated in rat liver mitochondria. but no protein has ever been associated with this activity. By using information derived from the phylogenetically distant yeast mitochondrial carrier for SAM and from related human expressed sequence tags. a human cDNA sequence was completed. This sequence was overexpressed in bacteria, and its product was purified. reconstituted into phospholipid vesicles and identified from its transport properties as the human mitochondrial SAM carrier (SAMC). Unlike the yeast orthologue SAMC catalysed virtually only countertransport, exhibited a higher transport affinity for SAM and was strongly inhibited by tannic acid and Bromocresol Purple. SAMC was found to be expressed in all human tissues examined and was localized to the mitochondria. The physiological role of SAMC is probably to exchange cytosolic SAM for mitochondrial S-adenosylhomocysteine. This is the first report describing the identification and characterization of the human SAMC and its gene.
引用
收藏
页码:183 / 190
页数:8
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