Publications

• Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes.

  Ramseier T.M., Winteler H.V., Hennecke H.

  We report the DNA sequence and mutational analysis of a novel cluster of six Bradyrhizobium japonicum genes of which at least three (designated cycV, cycW, and cycX) are essential for the formation of all cellular c-type cytochromes. Mutants having insertions in these genes were completely devoid ... >> More

  We report the DNA sequence and mutational analysis of a novel cluster of six Bradyrhizobium japonicum genes of which at least three (designated cycV, cycW, and cycX) are essential for the formation of all cellular c-type cytochromes. Mutants having insertions in these genes were completely devoid of any soluble (periplasmic) or membrane-bound c-type cytochromes; even the apo form of cytochrome c1 was not detectable, neither in the membrane nor in the soluble fraction. As a consequence, the mutants had pleiotropic phenotypes such as defects in nitrate respiration, H2 oxidation, electron transport to cytochrome alpha alpha 3, and microaerobic respiration during symbiosis. A fourth open reading frame (ORF132) encoded a protein that might also be concerned with cytochrome c formation, but perhaps only indirectly. The other two open reading frames did not appear to function in this process. The predicted amino acid sequences of the cycW and cycX gene products suggested that these proteins were membrane-bound. The cycV gene product showed extensive similarity to the ATP-binding subunit of a superfamily of membrane-associated transport systems. The predicted ORF132 product was strikingly similar to bacterial thioredoxins and eukaryotic protein disulfide isomerase. Based on these findings it is possible that these proteins are members of a complex transport system involved in the biogenesis of all cytochromes c. << Less

  J. Biol. Chem. 266:7793-7803(1991) [PubMed] [EuropePMC]

• Identification of a mammalian mitochondrial porphyrin transporter.

  Krishnamurthy P.C., Du G., Fukuda Y., Sun D., Sampath J., Mercer K.E., Wang J., Sosa-Pineda B., Murti K.G., Schuetz J.D.

  The movement of anionic porphyrins (for example, haem) across intracellular membranes is crucial to many biological processes, but their mitochondrial translocation and coordination with haem biosynthesis is not understood. Transport of porphyrins into isolated mitochondria is energy-dependent, as ... >> More

  The movement of anionic porphyrins (for example, haem) across intracellular membranes is crucial to many biological processes, but their mitochondrial translocation and coordination with haem biosynthesis is not understood. Transport of porphyrins into isolated mitochondria is energy-dependent, as expected for the movement of anions into a negatively charged environment. ATP-binding cassette transporters actively facilitate the transmembrane movement of substances. We found that the mitochondrial ATP-binding cassette transporter ABCB6 is upregulated (messenger RNA and protein in human and mouse cells) by elevation of cellular porphyrins and postulated that ABCB6 has a function in porphyrin transport. We also predicted that ABCB6 is functionally linked to haem biosynthesis, because its mRNA is found in both human bone marrow and CD71+ early erythroid cells (by database searching), and because our results show that ABCB6 is highly expressed in human fetal liver, and Abcb6 in mouse embryonic liver. Here we demonstrate that ABCB6 is uniquely located in the outer mitochondrial membrane and is required for mitochondrial porphyrin uptake. After ABCB6 is upregulated in response to increased intracellular porphyrin, mitochondrial porphyrin uptake activates de novo porphyrin biosynthesis. This process is blocked when the Abcb6 gene is silenced. Our results challenge previous assumptions about the intracellular movement of porphyrins and the factors controlling haem biosynthesis. << Less

  Nature 443:586-589(2006) [PubMed] [EuropePMC]

• orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria.

  Jekabsons W., Schuster W.

  A highly transcribed region in Oenothera mitochondria codes for an open reading frame comprising 250 condons (orf250). This open reading frame shows high sequence similarity to the helC gene of Rhodobacter capsulatus which encodes a subunit of a proposed ABC-type heme transporter. Transcripts of o ... >> More

  A highly transcribed region in Oenothera mitochondria codes for an open reading frame comprising 250 condons (orf250). This open reading frame shows high sequence similarity to the helC gene of Rhodobacter capsulatus which encodes a subunit of a proposed ABC-type heme transporter. Transcripts of orf250 are edited by cytidine to uridine transitions at 29 sites, altering 10% of all encoded amino acids. Genes homologous to helC have also been found in the bacteria Bradyrhizobium japonicum and Escherichia coli, and are conserved in mitochondria of Marchantia polymorpha, Daucus carota, and Arabidopsis thaliana. In bacteria these genes belong to operons that are involved in the biogenesis of c-type cytochromes. The bacterial gene organization is partly conserved in Marchantia, but altered in the mitochondrial genome of Oenothera. << Less

  Mol. Gen. Genet. 246:166-173(1995) [PubMed] [EuropePMC]

• Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya.

  Saier M.H. Jr.

  Although enzymes catalyzing chemical reactions have long been classified according to the system developed by the Enzyme Commission (EC), no comparable system has been developed or proposed for transport proteins catalyzing transmembrane vectorial reactions. We here propose a comprehensive system, ... >> More

  Although enzymes catalyzing chemical reactions have long been classified according to the system developed by the Enzyme Commission (EC), no comparable system has been developed or proposed for transport proteins catalyzing transmembrane vectorial reactions. We here propose a comprehensive system, designated the Transport Commission (TC) system, based both on function and phylogeny. The TC system initially categorizes permeases according to mode of transport and energy coupling mechanism, and each category is assigned a one-component TC number (W). The secondary level of classification corresponds to the phylogenetic family (or superfamily) to which a particular permease is assigned, and each family is assigned a two-component TC number (W.X). The third level of classification refers to the phylogenetic cluster within a family (or the family within a superfamily) to which the permease belongs, and each cluster receives a three-component TC number (W.X.Y). Finally, the last level of categorization is based on substrate specificity and polarity of transport, and each entry is assigned a four component TC number (W.X.Y.Z). This system is based on the observation that mode of transport and energy coupling mechanism are fundamental properties of transport systems that very seldom transcend familial lines, but substrate specificity, being readily alterable by point mutations, is a superficial characteristic that often transcends familial lines. The proposed system has the potential to include all known permeases for which sequence data are available and has the flexibility to accommodate the multitude of permeases likely to be revealed by future genome sequencing and biochemical analysis. Major conclusions resulting from our classification efforts are described. The classification system, which will be continuously updated, is available on our World Wide Web site (http:/(/)www-biology.ucsd.edu/ approximately msaier/transport/titlepage.html). << Less

  Adv Microb Physiol 40:81-136(1998) [PubMed] [EuropePMC]

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