The Mitochondrial Carrier Family of Transport Proteins: Structural, Functional, and Evolutionary Relationships

References

• Allard J. D., Bertrand K. P. Membrane topology of the pBR322 tetracycline resistance protein. TetAPhoA gene fusions and implications for the mechanism of TetA membrane insertion. J. Biol. Chem. 1992; 267: 17809–17819
   PubMedGoogle Scholar
• Aquila H., Eiermann W., Babel W., Klingenberg M. Isolation of the ADP/ATP translocator from beef heart mitochondria as the bongkrekate-protein complex. Eur. J. Biochem. 1978; 85: 549–560
   Google Scholar
• Aquila H., Link T. A., Klingenberg M. The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane. EMBO J. 1985; 4: 2369–2376
   PubMed Web of Science ®Google Scholar
• Aquila H., Link T. A., Klingenberg M. Solute carriers involved in energy transfer of mitochondria form a homologous protein family. FEBS Lett. 1987; 212: 1–9
   PubMed Web of Science ®Google Scholar
• Bairoch A. PROSITE: a dictionary of sites and patterns in proteins. Nucl. Acids Res. 1992; 20: 2013–2018
   PubMed Web of Science ®Google Scholar
• Beavis A. D., Vercesi A. E. Anion uniport in plant mitochondria is mediated by a Mg2+-insensitive inner membrane anion channel. J. Biol. Chem. 1992; 267: 3079–3087
   PubMed Web of Science ®Google Scholar
• Bisaccia F., DePalma A., Palmieri F. Identification and purification of the aspartate/glutamate carrier from bovine heart mitochondria. Biochim. Biophys. Acta 1992; 1106: 291–296
   Google Scholar
• Bogner W., Aquila H., Klingenberg M. The transmembrane arrangement of the ADP/ATP carrier as elucidated by the lysine reagent pyridoxal 5-phosphate. Eur. J. Biochem. 1986; 161: 611–620
   Google Scholar
• Bork P., Doolittle R. F. Proposed acquisition of an animal protein domain by bacteria. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 8990–8994
   Google Scholar
• Brooker R. J. The lactose permease of Escherichia coli. Res. Microbiol 1990; 141: 309–315
   PubMedGoogle Scholar
• Capobianco L., Brandolin G., Palmieri F. Transmembrane topography of the mitochondrial phosphate carrier explored by peptide-specific antibodies and enzymatic digestion. Biochemistry 1991; 30: 4963–4969
   Google Scholar
• Colombini M. Regulation of the mitochondrial outer membrane channel. VDAC J. Bioenerg. Biomembr. 1987; 19: 309–320
   Google Scholar
• Cowan S. W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R. A., Jansonius J. N., Rosenbusch J. P. Crystal structures explain functional properties of two E. coli porins. Nature 1992; 358: 727–733
   PubMed Web of Science ®Google Scholar
• Dayhoff M. O., Barker W. C., Hunt L. T. Establishing homologies in protein sequences. Meth. Enzymol. 1983; 91: 524–545
   PubMed Web of Science ®Google Scholar
• De Hoop M. J., Ab G. Import of proteins into peroxisomes and other microbodies. Biochem. J. 1992; 286: 657–669
   PubMed Web of Science ®Google Scholar
• Devereux J., Haeberli P., Smithies N. O. A comprehensive set of sequence analyses for the VAX. Nucl. Acids Res. 1984; 12: 387–395
   PubMed Web of Science ®Google Scholar
• Dierks T., Riemer E., Krämer R. Reaction mechanism of the reconstituted aspartate/glutamate carrier from bovine heart mitochondria. Biochim. Biophys. Acta 1988; 943: 231–244
   Google Scholar
• Dierks T., Salentin A., Heberger C., Krämer R. The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SH-reagents. Biochim. Biophys. Acta 1990a; 1028: 268–280
   PubMedGoogle Scholar
• Dierks T., Salentin A., Krämer R. Pore-like and carrier-like properties of the mitochondrial aspartate/glutamate carrier after modification by SH-reagents: evidence for a preformed channel as a structural requirement of carrier-mediated transport. Biochim. Biophys. Acta 1990b; 1028: 281–288
   Google Scholar
• Dingwall C., Laskey R. A. Nuclear targeting sequences a consensus. TIBS 1991; 16: 478–481
   PubMed Web of Science ®Google Scholar
• Doolittle R. F. Similar amino acid sequences: chance or common ancestry. Science 1981; 214: 149–159
   PubMed Web of Science ®Google Scholar
• Doolittle R.F. Of Urfs and Orfs. University Science Books, Mill Valley, CA. 1986
   Google Scholar
• Doolittle R. F. Reconstructing history with amino acid sequences. Prot. Sci. 1992; 1: 191–200
   Google Scholar
• Doolittle R. F., Feng D. F. A nearest neighbor procedure for relating progressively aligned amino acid sequences. Meth. Enzymol. 1990; 183: 659–669
   Google Scholar
• Feng D. F., Doolittle R. F. Progressive alignment and phylogenetic tree construction of protein sequences. Meth. Enzymol. 1990; 183: 375–387
   PubMed Web of Science ®Google Scholar
• Garlid K. D., Shariat-Madar Z., Nath S., Jezek P. Reconstitution and partial purification of the Na+-selective Na+/H+ antiporter of beef heart mitochondria. J. Biol. Chem. 1991; 266: 6518–6523
   Google Scholar
• Gawaz M., Douglas M. G., Klingenberg M. Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast. J. Biol. Chem. 1990; 265: 14202–14208
   PubMed Web of Science ®Google Scholar
• Griffith J. K., Baker M. E., Rouch D. A., Page M. G. P., Skurray R. A., Paulsen I. T., Chater K. F., Baldwin S. A., Henderson P. J. F. Membrane transport proteins: implications of sequence comparisons. Curr. Opin. Cell Biol. 1992; 4: 684–695
   PubMedGoogle Scholar
• Henderson P. J. F. The homologous glucose transport proteins of prokaryotes and eukaryotes. Res. Microbiol. 1990; 141: 316–328
   PubMedGoogle Scholar
• Herrick G., Cartinhour S., Dawson D., Ang D., Sheets R., Lee A., Williams K. Mobile elements bounded by C-4-A-4 telomeric repeats in Oxytricha fallax. Cell 1985; 43: 759–768
   PubMedGoogle Scholar
• Herrick G., Cartinhour S. W., Williams K. R., Kotter K. P. Multiple sequence versions of the Oxytricha fallax 81-MAC processing family. J. Protozool. 1987; 34: 429–434
   Google Scholar
• Kaback H. R. Molecular biology of active transport: from membrane to molecule to mechanism. The Harvey Lectures. Series 83, Alan R. Liss, New York 1989; 77–105
   Google Scholar
• Klaus S., Casteilla L., Bouillaud F., Ricquier D. The uncoupling protein UCP: a membraneous mitochondrial ion carrier exclusively expressed in brown adipose tissue. Int. J. Biochem. 1991; 23: 791–801
   PubMedGoogle Scholar
• Klingenberg M. Membrane protein oligomeric structure and transport function. Nature 1981; 290: 449–454
   PubMed Web of Science ®Google Scholar
• Klingenberg M. Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 1989; 270: 1–14
   PubMedGoogle Scholar
• Klingenberg M. Mechanism and evolution of the uncoupling protein of brown adipose tissue. TIBS 1990; 15: 108–112
   PubMedGoogle Scholar
• Klingenberg M., Appel M. The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups. Eur. J. Biochem. 1989; 180: 123–131
   Google Scholar
• Klingenberg M., Winkler E. The reconstituted isolated uncoupling protein is a membrane potential driven H+ translocator. EMBO J. 1985; 4: 3087–3092
   Google Scholar
• Knirsch M., Gawaz M. P., Klingenberg M. The isolation and reconstitution of the ADP/ATP carrier from wild-type Saccharomyces cerevisiae Identification of primarily one type (AAC-2). FEBS Lett. 1989; 244: 427–432
   Google Scholar
• Krämer R., Klingenberg M. Reconstitution of adenine nucleotide transport with purified ADP, ATP-carrier protein. FEBS Lett. 1977; 82: 363–367
   Google Scholar
• Kyte J., Doolittle R. F. A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 1982; 157: 105–132
   PubMed Web of Science ®Google Scholar
• LaNoue K. F., Schoolwerth A. C. Metabolite transport in mitochondria. Ann. Rev. Biochem. 1979; 48: 871–922
   PubMed Web of Science ®Google Scholar
• Lipman D. J., Pearson W. R. Rapid and sensitive protein similarity searches. Science 1985; 227: 1435–1441
   PubMed Web of Science ®Google Scholar
• Lunardi J., Attardi G. Differential regulation of expression of the multiple ADP/ATP translocase genes in human cells. J. Biol. Chem. 1991; 266: 16534–16540
   Google Scholar
• Lunardi J., Hurko O., Engel W. K., Attardi G. The multiple ADP/ATP translocase genes are differentially expressed during human muscle development. J. Biol. Chem. 1992; 267: 15267–15270
   Google Scholar
• Maloney P. C. A consensus structure for membrane transport. Res. Microbiol. 1990; 141: 374–383
   Google Scholar
• Mannella C. A. The “ins” and “outs” of mitochondrial membrane channels. TIBS 1992; 17: 315–320
   Google Scholar
• Marger M. D., Saier M. H., Jr. A major super-family of transmembrane facilitators catalyzing uniport, symport and antiport. TIBS 1993; 18: 13–20
   PubMed Web of Science ®Google Scholar
• McCammon M. T., Dowds C. A., Orth K., Moomaw C. R., Slaughter C. A., Goodman J. M. Sorting of peroxisomal membrane protein PMP47 from Candida into peroxisomal membranes of Saccharomyces cerevisiae. J. Biol. Chem. 1990; 265: 20098–20105
   PubMedGoogle Scholar
• Mitchell P. Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems. Eur. J. Biochem. 1979; 95: 1–20
   PubMedGoogle Scholar
• Nicholls D. G. Hamster brown-adipose-tissue mitochondria. Purine nucleotide control of the ion conductance of the inner membrane, the nature of the nucleotide binding site. Eur. J. Biochem. 1976; 62: 223–228
   Google Scholar
• Nikaido H. Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 1992; 6: 435–442
   PubMed Web of Science ®Google Scholar
• Nikaido H., Saier M. H., Jr. Transport proteins in bacteria: common themes in their design. Science 1992; 258: 936–942
   Google Scholar
• Palmieri F., Bisaccia F., Capobianco L., Iacobazzi V., Indiveri C., Zara V. Structural and functional properties of mitochondrial anion carriers. Biochim. Biophys. Acta 1990; 1018: 147–150
   Google Scholar
• Palmieri F., Bisaccia F., Iacobazzi V., Indiveri C., Zara V. Mitochondrial substrate carriers. Biochim. Biophys. Acta 1992; 1101: 223–227
   Google Scholar
• Pao G. M., Wu L. F., Johnson K. D., Höfte H., Chrispeels M. J., Sweet G., Sandal N. N., Saier M. H., Jr. Evolution of the MIP family of integral membrane transport proteins. Mol. Microbiol. 1991; 5: 33–37
   PubMed Web of Science ®Google Scholar
• Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. U.S.A. 1988; 85: 2444–2448
   PubMed Web of Science ®Google Scholar
• Pratt R. D., Ferreira G. C., Pedersen P. L. Mitochondrial phosphate transport. Import of the H+/Pi symporter and role of the presequence. J. Biol. Chem. 1991; 266: 1276–1280
   Google Scholar
• Reizer A., Pao G. M., Saier M. H., Jr. Evolutionary relationships between the permease proteins of the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Construction of phylogenetic trees and possible relatedness to proteins of eukaryotic mitochondria. J. Mol. Evol. 1991; 33: 179–193
   Google Scholar
• Reizer J., Reizer A., Saier M. H., Jr. The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit. Rev. Biochem. Mol. Biol 1993; 28: 235–257
   PubMed Web of Science ®Google Scholar
• Roepe P. D., Consler T. G., Menezes M. E., Kaback H. R. The lac permease of Escherichia coli: site-directed mutagenesis studies on the mechanism of β-galactoside/H+ symport. Res. Microbiol. 1991; 141: 290–308
   Google Scholar
• Runswick M. J., Powell S. J., Nyren P., Walker J. E. Sequence of the bovine mitochondrial phosphate carrier proteins: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein. EMBO J. 1987; 6: 1367–1373
   PubMed Web of Science ®Google Scholar
• Runswick M. J., Walker J. E., Bisaccia F., Iacobazzi V., Palmieri F. Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural relationship to other mitochondrial transport proteins. Biochemistry 1990; 29: 11033–11040
   PubMed Web of Science ®Google Scholar
• Saier M. H., Jr. Enzymes in Metabolic Pathways: A Comparative Study of Mechanism, Structure, Evolution, and Control. Harper & Row, New York 1987
   Google Scholar
• Saier M. H., Jr. Evolution of permease diversity and energy-coupling mechanisms: an introduction. Res. Microbiol 1990; 141: 281–286
   Google Scholar
• Saier M. H., Jr., Reizer J. Families and super-families of transport proteins common to prokaryotes and eukaryotes. Curr. Opin. Struct. Biol 1991; 1: 362–368
   Google Scholar
• Saier M. H., Jr., Werner P. K., Müller M. Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process. Microbiol. Rev. 1989; 53: 333–366
   PubMedGoogle Scholar
• Saier M. H., Jr., Wu L. F., Sweet G., Reizer A., Reizer J. Evolution of permease diversity and energy coupling mechanisms with special reference to the bacterial phosphotransferase system. Biochim. Biophys. Acta 1990; 1018: 248–251
   Google Scholar
• Saier M. H., Jr., Reizer A., Pao G. M., Wu L. F., Reizer J., Romano A. H. Evolution of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. II. Molecular considerations. The Evolution of Metabolic Function, R. P. Mortlock. CRC Press, Boca Raton, FL 1992; 171–204
   Google Scholar
• Smith D. W. A complete and integrated system for DNA protein sequence analysis using VAX/VMS computers. CA-BIOS 1988; 4: 212
   Google Scholar
• Sullivan T. D., Strelow L. I., Illingworth C. A., Phillips R. L., Nelson O. E., Jr. Analysis of the maize brittle-1 alleles and a defective suppressor-mutator induced mutable allele. Plant Cell 1991; 3: 1337–1348
   Google Scholar
• Trandinh C. C., Pao G. M., Saier M. H., Jr. Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases. FASEB J. 1992; 6: 3410–3420
   Google Scholar
• Troll H., Malchow D., Müller-Taubenberger A., Humbel B., Lottspeich F., Ecke M., Gerisch G., Schmid A., Benz R. Purification, functional characterization, and cDNA sequencing of mitochondrial porin from Dictyostelium discoideum. J. Biol. Chem. 1992; 267: 21072–21079
   Google Scholar
• Vartak N. B., Reizer J., Reizer A., Gripp J. T., Groisman E. A., Wu L. F., Tomich J. M., Saier M. H., Jr. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Res. Microbiol 1991; 142: 951–963
   Google Scholar
• von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol 1992; 225: 487–494
   PubMed Web of Science ®Google Scholar
• Wiesenberger G., Link T. A., von Ahsen U., Waldherr M., Schweyen R. J. MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast, are new members of the mitochondrial carrier family. Nuclear Gene Products Affecting Mitochondrial RNA, P. Chambon. Academic Press, New York 1991; 23–37
   Google Scholar
• Winkler E., Klingenberg M. An improved procedure for reconstitution of the uncoupling protein and in-depth analysis of H+/OH transport. Eur. J. Biochem. 1992; 207: 135–145
   Google Scholar
• Yu Y. G., Weiss R. L. Arginine transport in mitochondria of Neurospora crassa. J. Biol. Chem 1992; 267: 15491–15495
   Google Scholar
• Zarrilli R., Oates E. L., McBride O. W., Lerman M. I., Chan J. Y., Santisteban P., Ursini M. V., Notkins A. L., Kohn L. D. Sequence and chromosomal assignment of a novel cDNA identified by immunoscreening of a thyroid expression library: similarity to a family of mitochondrial solute carrier proteins. Mol. Endocrinol 1989; 3: 1498–1508
   PubMedGoogle Scholar