메뉴 건너뛰기




Volumn 396, Issue 9-10, 2015, Pages 955-966

Structure, function, evolution, and application of bacterial Pnu-type vitamin transporters

Author keywords

membrane transport; Pnu transporters; vitamins

Indexed keywords

BACTERIAL PROTEIN; PYRIDINE NUCLEOTIDE; VITAMIN; CARRIER PROTEIN;

EID: 84937531605     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2015-0113     Document Type: Review
Times cited : (18)

References (64)
  • 1
    • 0035937113 scopus 로고    scopus 로고
    • Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor
    • Andersen, R.B. and Neuhard, J. (2001). Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor. J. Biol. Chem. 276, 5518-5524.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5518-5524
    • Andersen, R.B.1    Neuhard, J.2
  • 4
    • 0023414724 scopus 로고
    • Genetic characterization and regulation of the nadB locus of Salmonella typhimurium
    • Cookson, B.T., Olivera, B.M., and Roth, J.R. (1987). Genetic characterization and regulation of the nadB locus of Salmonella typhimurium. J. Bacteriol. 169, 4285-4293.
    • (1987) J. Bacteriol. , vol.169 , pp. 4285-4293
    • Cookson, B.T.1    Olivera, B.M.2    Roth, J.R.3
  • 5
    • 0023732833 scopus 로고
    • Utilization and metabolism of NAD by Haemophilus parainfluenzae
    • Cynamon, M.H., Sorg, T.B., and Patapow, A. (1988). Utilization and metabolism of NAD by Haemophilus parainfluenzae. J. Gen. Microbiol. 134, 2789-2799.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2789-2799
    • Cynamon, M.H.1    Sorg, T.B.2    Patapow, A.3
  • 6
    • 11244273057 scopus 로고    scopus 로고
    • Role of human nucleoside transporters in the cellular uptake of two inhibitors of IMP dehydrogenase, tiazofurin and benzamide riboside
    • Damaraju, V.L., Visser, F., Zhang, J., Mowles, D., Ng, A.M.L., Young, J.D., Jayaram, H.N., and Cass, C.E. (2005). Role of human nucleoside transporters in the cellular uptake of two inhibitors of IMP dehydrogenase, tiazofurin and benzamide riboside. Mol. Pharmacol. 67, 273-279.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 273-279
    • Damaraju, V.L.1    Visser, F.2    Zhang, J.3    Mowles, D.4    Ng, A.M.L.5    Young, J.D.6    Jayaram, H.N.7    Cass, C.E.8
  • 7
  • 9
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: A maximum likelihood approach
    • Felsenstein, J. (1981). Evolutionary trees from DNA sequences: a maximum likelihood approach. J. Mol. Evol. 17, 368-376.
    • (1981) J. Mol. Evol. , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 10
    • 84877878130 scopus 로고    scopus 로고
    • Directed evolution of an E. Coli inner membrane transporter for improved efflux of biofuel molecules
    • Foo, J.L. and Leong, S.S.J. (2013). Directed evolution of an E. coli inner membrane transporter for improved efflux of biofuel molecules. Biotechnol. Biofuels 6, 81.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 81
    • Foo, J.L.1    Leong, S.S.J.2
  • 11
    • 84872781515 scopus 로고    scopus 로고
    • Structural biology. (Pseudo-)symmetrical transport
    • Forrest, L.R. (2013). Structural biology. (Pseudo-)symmetrical transport. Science 339, 399-401.
    • (2013) Science , vol.339 , pp. 399-401
    • Forrest, L.R.1
  • 12
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest, L.R., Krämer, R., and Ziegler, C. (2011). The structural basis of secondary active transport mechanisms. Biochim. Biophys. Acta 1807, 167-188.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Krämer, R.2    Ziegler, C.3
  • 13
    • 85046521617 scopus 로고
    • The bifunctional NadR regulator of Salmonella typhimurium: Location of regions involved with DNA binding, nucleotide transport and intramolecular communication
    • Foster, J.W. and Penfound, T. (1993). The bifunctional NadR regulator of Salmonella typhimurium: location of regions involved with DNA binding, nucleotide transport and intramolecular communication. FEMS Microbiol. Lett. 112, 179-183.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 179-183
    • Foster, J.W.1    Penfound, T.2
  • 14
    • 0023355786 scopus 로고
    • Regulation of NAD metabolism in Salmonella typhimurium: Genetic analysis and cloning of the nadR repressor locus
    • Foster, J.W., Holley-Guthrie, E.A., and Warren, F. (1987). Regulation of NAD metabolism in Salmonella typhimurium: genetic analysis and cloning of the nadR repressor locus. Mol. Gen. Genet. 208, 279-287.
    • (1987) Mol. Gen. Genet. , vol.208 , pp. 279-287
    • Foster, J.W.1    Holley-Guthrie, E.A.2    Warren, F.3
  • 15
    • 0025285684 scopus 로고
    • Regulation of NAD metabolism in Salmonella typhimu-rium: Molecular sequence analysis of the bifunctional nadR regulator and the nadA-pnuC operon
    • Foster, J.W., Park, Y.K., Penfound, T., Fenger, T., and Spector, M.P. (1990). Regulation of NAD metabolism in Salmonella typhimu-rium: molecular sequence analysis of the bifunctional nadR regulator and the nadA-pnuC operon. J. Bacteriol. 172, 4187-4196.
    • (1990) J. Bacteriol. , vol.172 , pp. 4187-4196
    • Foster, J.W.1    Park, Y.K.2    Penfound, T.3    Fenger, T.4    Spector, M.P.5
  • 16
    • 38849104227 scopus 로고    scopus 로고
    • Comparative genomics and functional annotation of bacterial transporters
    • Gelfand, M.S. and Rodionov, D.A. (2008). Comparative genomics and functional annotation of bacterial transporters. Phys. Life Rev. 5, 22-49.
    • (2008) Phys. Life Rev. , vol.5 , pp. 22-49
    • Gelfand, M.S.1    Rodionov, D.A.2
  • 17
    • 22544445194 scopus 로고    scopus 로고
    • Evolution of the NadR regulon in Enterobacteriaceae
    • Gerasimova, A.V. and Gelfand, M.S. (2005). Evolution of the NadR regulon in Enterobacteriaceae. J. Bioinform. Comput. Biol. 3, 1007-1019.
    • (2005) J. Bioinform. Comput. Biol. , vol.3 , pp. 1007-1019
    • Gerasimova, A.V.1    Gelfand, M.S.2
  • 18
    • 33749347331 scopus 로고    scopus 로고
    • + utilization in Pasteurel-laceae: Simplification of a complex pathway
    • + utilization in Pasteurel-laceae: simplification of a complex pathway. J. Bacteriol. 188, 6719-6727.
    • (2006) J. Bacteriol. , vol.188 , pp. 6719-6727
    • Gerlach, G.1    Reidl, J.2
  • 19
    • 0025158574 scopus 로고
    • In vitro evaluation of nicotinamide riboside analogs against Haemophilus influenzae
    • Godek, C.P. and Cynamon, M.H. (1990). In vitro evaluation of nicotinamide riboside analogs against Haemophilus influenzae. Antimicrob. Agents Chemother. 34, 1473-1479.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 1473-1479
    • Godek, C.P.1    Cynamon, M.H.2
  • 20
    • 39749093132 scopus 로고    scopus 로고
    • The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
    • Grill, S., Busenbender, S., Pfeiffer, M., Köhler, U., and Mack, M. (2008). The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin. J. Bacteriol. 190, 1546-1553.
    • (2008) J. Bacteriol. , vol.190 , pp. 1546-1553
    • Grill, S.1    Busenbender, S.2    Pfeiffer, M.3    Köhler, U.4    MacK, M.5
  • 21
    • 16844384577 scopus 로고    scopus 로고
    • Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica
    • Grose, J.H., Bergthorsson, U., and Roth, J.R. (2005a). Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica. J. Bacteriol. 187, 2774-2782.
    • (2005) J. Bacteriol. , vol.187 , pp. 2774-2782
    • Grose, J.H.1    Bergthorsson, U.2    Roth, J.R.3
  • 22
    • 21144437936 scopus 로고    scopus 로고
    • Assimilation of nicotinamide mononu-cleotide requires periplasmic AphA phosphatase in Salmonella enterica
    • Grose, J.H., Bergthorsson, U., Xu, Y., Sterneckert, J., Khodaverdian, B., and Roth, J.R. (2005b). Assimilation of nicotinamide mononu-cleotide requires periplasmic AphA phosphatase in Salmonella enterica. J. Bacteriol. 187, 4521-4530.
    • (2005) J. Bacteriol. , vol.187 , pp. 4521-4530
    • Grose, J.H.1    Bergthorsson, U.2    Xu, Y.3    Sterneckert, J.4    Khodaverdian, B.5    Roth, J.R.6
  • 23
    • 82455188342 scopus 로고    scopus 로고
    • RibM from Streptomyces davawensis is a riboflavin/roseoflavin transporter and may be useful for the optimization of riboflavin production strains
    • Hemberger, S., Pedrolli, D.B., Stolz, J., Vogl, C., Lehmann, M., and Mack, M. (2011). RibM from Streptomyces davawensis is a riboflavin/roseoflavin transporter and may be useful for the optimization of riboflavin production strains. BMC Biotechnol. 11, 119.
    • (2011) BMC Biotechnol. , vol.11 , pp. 119
    • Hemberger, S.1    Pedrolli, D.B.2    Stolz, J.3    Vogl, C.4    Lehmann, M.5    MacK, M.6
  • 25
    • 84921020525 scopus 로고    scopus 로고
    • Diversity of membrane transport proteins for vitamins in bacteria and archaea
    • Jaehme, M. and Slotboom, D.J. (2015). Diversity of membrane transport proteins for vitamins in bacteria and archaea. Biochim. Biophys. Acta 1850, 565-576.
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 565-576
    • Jaehme, M.1    Slotboom, D.J.2
  • 26
    • 84908869634 scopus 로고    scopus 로고
    • Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog
    • Jaehme, M., Guskov, A., and Slotboom, D.J. (2014). Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog. Nat. Struct. Mol. Biol. 21, 1013-1015.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 1013-1015
    • Jaehme, M.1    Guskov, A.2    Slotboom, D.J.3
  • 27
    • 38549163808 scopus 로고    scopus 로고
    • Mutagenesis studies on TenA: A thiamin salvage enzyme from Bacillus subtilis
    • Jenkins, A.L., Zhang, Y., Ealick, S.E., and Begley, T.P. (2008). Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis. Bioorg. Chem. 36, 29-32.
    • (2008) Bioorg. Chem. , vol.36 , pp. 29-32
    • Jenkins, A.L.1    Zhang, Y.2    Ealick, S.E.3    Begley, T.P.4
  • 28
    • 84926471531 scopus 로고    scopus 로고
    • When two turn into one: Evolution of membrane transporters from half modules
    • Keller, R., Ziegler, C., and Schneider, D. (2014). When two turn into one: evolution of membrane transporters from half modules. Biol. Chem. 395, 1379-1388.
    • (2014) Biol. Chem. , vol.395 , pp. 1379-1388
    • Keller, R.1    Ziegler, C.2    Schneider, D.3
  • 29
    • 0034968382 scopus 로고    scopus 로고
    • NadN and e (P4) are essential for utilization of NAD and nicotinamide mononucleotide but not nicotinamide riboside in Haemophilus influenzae
    • Kemmer, G., Reilly, T.J., Schmidt-Brauns, J., Zlotnik, G.W., Green, B.A., Fiske, M.J., Herbert, M., Kraiss, A., Schlör, S., Smith, A., et al. (2001). NadN and e (P4) are essential for utilization of NAD and nicotinamide mononucleotide but not nicotinamide riboside in Haemophilus influenzae. J. Bacteriol. 183, 3974-3981.
    • (2001) J. Bacteriol. , vol.183 , pp. 3974-3981
    • Kemmer, G.1    Reilly, T.J.2    Schmidt-Brauns, J.3    Zlotnik, G.W.4    Green, B.A.5    Fiske, M.J.6    Herbert, M.7    Kraiss, A.8    Schlör, S.9    Smith, A.10
  • 30
    • 0018570672 scopus 로고
    • Pyridine nucleo-tide cycle of Salmonella typhimurium: In vitro demonstration of nicotinamide mononucleotide deamidase and characterization of pnuA mutants defective in nicotinamide mononucleotide transport
    • Kinney, D.M., Foster, J.W., and Moat, A.G. (1979). Pyridine nucleo-tide cycle of Salmonella typhimurium: in vitro demonstration of nicotinamide mononucleotide deamidase and characterization of pnuA mutants defective in nicotinamide mononucleotide transport. J. Bacteriol. 140, 607-611.
    • (1979) J. Bacteriol. , vol.140 , pp. 607-611
    • Kinney, D.M.1    Foster, J.W.2    Moat, A.G.3
  • 31
    • 0036947230 scopus 로고    scopus 로고
    • Ribosylnicotinamide kinase domain of NadR protein: Identification and implications in NAD biosynthesis
    • Kurnasov, O.V., Polanuyer, B.M., Ananta, S., Sloutsky, R., Tam, A., Gerdes, S.Y., and Osterman, A.L. (2002). Ribosylnicotinamide kinase domain of NadR protein: identification and implications in NAD biosynthesis. J. Bacteriol. 184, 6906-6917.
    • (2002) J. Bacteriol. , vol.184 , pp. 6906-6917
    • Kurnasov, O.V.1    Polanuyer, B.M.2    Ananta, S.3    Sloutsky, R.4    Tam, A.5    Gerdes, S.Y.6    Osterman, A.L.7
  • 32
    • 84883306665 scopus 로고    scopus 로고
    • Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli
    • Langer, S., Hashimoto, M., Hobl, B., Mathes, T., and Mack, M. (2013). Flavoproteins are potential targets for the antibiotic roseoflavin in Escherichia coli. J. Bacteriol. 195, 4037-4045.
    • (2013) J. Bacteriol. , vol.195 , pp. 4037-4045
    • Langer, S.1    Hashimoto, M.2    Hobl, B.3    Mathes, T.4    MacK, M.5
  • 33
    • 84903271929 scopus 로고    scopus 로고
    • Directed evolution of a cellodextrin transporter for improved biofuel production under anaerobic conditions in Saccharomyces cerevisiae
    • Lian, J., Li, Y., HamediRad, M., and Zhao, H. (2014). Directed evolution of a cellodextrin transporter for improved biofuel production under anaerobic conditions in Saccharomyces cerevisiae. Biotechnol. Bioeng. 111, 1521-1531.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1521-1531
    • Lian, J.1    Li, Y.2    HamediRad, M.3    Zhao, H.4
  • 34
    • 0020403651 scopus 로고
    • Nucleoside salvage pathway for NAD biosynthesis in Salmonella typhimurium
    • Liu, G., Foster, J., Manlapaz-Ramos, P., and Olivera, B.M. (1982). Nucleoside salvage pathway for NAD biosynthesis in Salmonella typhimurium. J. Bacteriol. 152, 1111-1116.
    • (1982) J. Bacteriol. , vol.152 , pp. 1111-1116
    • Liu, G.1    Foster, J.2    Manlapaz-Ramos, P.3    Olivera, B.M.4
  • 35
    • 33745488371 scopus 로고    scopus 로고
    • Riboflavin analogs and inhibitors of riboflavin biosynthesis
    • Mack, M. and Grill, S. (2006). Riboflavin analogs and inhibitors of riboflavin biosynthesis. Appl. Microbiol. Biotechnol. 71, 265-275.
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 265-275
    • MacK, M.1    Grill, S.2
  • 37
    • 58549088979 scopus 로고    scopus 로고
    • In vivo generation of flavoproteins with modified cofactors
    • Mathes, T., Vogl, C., Stolz, J., and Hegemann, P. (2009). In vivo generation of flavoproteins with modified cofactors. J. Mol. Biol. 385, 1511-1518.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1511-1518
    • Mathes, T.1    Vogl, C.2    Stolz, J.3    Hegemann, P.4
  • 38
    • 21144447964 scopus 로고    scopus 로고
    • + biosynthesis and nicotinamide ribosyl transport: Characterization of NadR ribonucleotide kinase mutants of Haemophilus influenzae
    • + biosynthesis and nicotinamide ribosyl transport: characterization of NadR ribonucleotide kinase mutants of Haemophilus influenzae. J. Bacteriol. 187, 4410-4420.
    • (2005) J. Bacteriol. , vol.187 , pp. 4410-4420
    • Merdanovic, M.1    Sauer, E.2    Reidl, J.3
  • 39
    • 84988807185 scopus 로고    scopus 로고
    • Engineering of an endogenous hex-ose transporter into a specific d-xylose transporter facilitates glucose-xylose co-consumption in Saccharomyces cerevisiae
    • Nijland, J.G., Shin, H.Y., de Jong, R.M., de Waal, P.P., Klaassen, P., and Driessen, A.J. (2014). Engineering of an endogenous hex-ose transporter into a specific d-xylose transporter facilitates glucose-xylose co-consumption in Saccharomyces cerevisiae. Biotechnol. Biofuels 7, 168.
    • (2014) Biotechnol. Biofuels , vol.7 , pp. 168
    • Nijland, J.G.1    Shin, H.Y.2    De Jong, R.M.3    De Waal, P.P.4    Klaassen, P.5    Driessen, A.J.6
  • 40
    • 79957549799 scopus 로고    scopus 로고
    • Pathways and subcellular compartmentation of NAD biosynthesis in human cells: From entry of extracellular precursors to mitochondrial NAD generation
    • Nikiforov, A., Dölle, C., Niere, M., and Ziegler, M. (2011). Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation. J. Biol. Chem. 286, 21767-21778.
    • (2011) J. Biol. Chem. , vol.286 , pp. 21767-21778
    • Nikiforov, A.1    Dölle, C.2    Niere, M.3    Ziegler, M.4
  • 41
    • 0042922793 scopus 로고    scopus 로고
    • Levels of nicotinamide adenine dinucleotide in extracellular body fluids of pigs may be growth-limiting for Actinobacillus pleuropneumoniae and Haemophilus parasuis
    • O'Reilly, T. and Niven, D.F. (2003). Levels of nicotinamide adenine dinucleotide in extracellular body fluids of pigs may be growth-limiting for Actinobacillus pleuropneumoniae and Haemophilus parasuis. Can. J. Vet. Res. 67, 229-231.
    • (2003) Can. J. Vet. Res. , vol.67 , pp. 229-231
    • O'Reilly, T.1    Niven, D.F.2
  • 43
    • 0032925513 scopus 로고    scopus 로고
    • NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typh-imurium
    • Penfound, T. and Foster, J.W. (1999). NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typh-imurium. J. Bacteriol. 181, 648-655.
    • (1999) J. Bacteriol. , vol.181 , pp. 648-655
    • Penfound, T.1    Foster, J.W.2
  • 44
    • 0030846927 scopus 로고    scopus 로고
    • Characterization of nicotina-mide mononucleotide adenylyltransferase from thermophilic archaea
    • Raffaelli, N., Pisani, F.M., Lorenzi, T., Emanuelli, M., Amici, A., Ruggieri, S., and Magni, G. (1997). Characterization of nicotina-mide mononucleotide adenylyltransferase from thermophilic archaea. J. Bacteriol. 179, 7718-7723.
    • (1997) J. Bacteriol. , vol.179 , pp. 7718-7723
    • Raffaelli, N.1    Pisani, F.M.2    Lorenzi, T.3    Emanuelli, M.4    Amici, A.5    Ruggieri, S.6    Magni, G.7
  • 45
    • 74049128960 scopus 로고    scopus 로고
    • An evolved xylose transporter from Zymomonas mobilis enhances sugar transport in Escherichia coli
    • Ren, C., Chen, T., Zhang, J., Liang, L., and Lin, Z. (2009). An evolved xylose transporter from Zymomonas mobilis enhances sugar transport in Escherichia coli. Microb. Cell Fact. 8, 66.
    • (2009) Microb. Cell Fact. , vol.8 , pp. 66
    • Ren, C.1    Chen, T.2    Zhang, J.3    Liang, L.4    Lin, Z.5
  • 46
    • 20644446065 scopus 로고    scopus 로고
    • Identification of a bacterial regulatory system for ribonucleotide reductases by phylo-genetic profiling
    • Rodionov, D.A. and Gelfand, M.S. (2005). Identification of a bacterial regulatory system for ribonucleotide reductases by phylo-genetic profiling. Trends Genet. 21, 385-389.
    • (2005) Trends Genet. , vol.21 , pp. 385-389
    • Rodionov, D.A.1    Gelfand, M.S.2
  • 47
    • 2242446202 scopus 로고    scopus 로고
    • Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms
    • Rodionov, D.A., Vitreschak, A.G., Mironov, A.A., and Gelfand, M.S. (2002). Comparative genomics of thiamin biosynthesis in procaryotes. New genes and regulatory mechanisms. J. Biol. Chem. 277, 48949-48959.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48949-48959
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 50
    • 9644301034 scopus 로고    scopus 로고
    • PnuC and the utilization of the nicotinamide riboside analog 3-aminopyridine in Haemophilus influenzae
    • Sauer, E., Merdanovic, M., Mortimer, A.P., Bringmann, G., and Reidl, J. (2004). PnuC and the utilization of the nicotinamide riboside analog 3-aminopyridine in Haemophilus influenzae. Antimicrob. Agents Chemother. 48, 4532-4541.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4532-4541
    • Sauer, E.1    Merdanovic, M.2    Mortimer, A.P.3    Bringmann, G.4    Reidl, J.5
  • 51
    • 84892670970 scopus 로고    scopus 로고
    • Structural and mechanistic insights into prokaryotic energy-coupling factor transporters
    • Slotboom, D.J. (2014). Structural and mechanistic insights into prokaryotic energy-coupling factor transporters. Nat. Rev. Microbiol. 12, 79-87.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 79-87
    • Slotboom, D.J.1
  • 52
    • 0021886181 scopus 로고
    • Genetic characterization of pyridine nucleotide uptake mutants of Salmonella typhimurium
    • Spector, M.P., Hill, J.M., Holley, E.A., and Foster, J.W. (1985). Genetic characterization of pyridine nucleotide uptake mutants of Salmonella typhimurium. J. Gen. Microbiol. 131, 1313-1322.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 1313-1322
    • Spector, M.P.1    Hill, J.M.2    Holley, E.A.3    Foster, J.W.4
  • 53
    • 0022483502 scopus 로고
    • Genetics of NAD metabolism in Salmonella typhimurium and cloning of the nadA and pnuC loci
    • Tirgari, S., Spector, M.P., and Foster, J.W. (1986). Genetics of NAD metabolism in Salmonella typhimurium and cloning of the nadA and pnuC loci. J. Bacteriol. 167, 1086-1088.
    • (1986) J. Bacteriol. , vol.167 , pp. 1086-1088
    • Tirgari, S.1    Spector, M.P.2    Foster, J.W.3
  • 54
    • 0037100667 scopus 로고    scopus 로고
    • Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation
    • Vitreschak, A.G., Rodionov, D.A., Mironov, A.A., and Gelfand, M.S. (2002). Regulation of riboflavin biosynthesis and transport genes in bacteria by transcriptional and translational attenuation. Nucleic Acids Res. 30, 3141-3151.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3141-3151
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 55
    • 0347418195 scopus 로고    scopus 로고
    • Riboswitches: The oldest mechanism for the regulation of gene expression?
    • Vitreschak, A.G., Rodionov, D.A., Mironov, A.A., and Gelfand, M.S. (2004). Riboswitches: the oldest mechanism for the regulation of gene expression? Trends Genet. 20, 44-50.
    • (2004) Trends Genet. , vol.20 , pp. 44-50
    • Vitreschak, A.G.1    Rodionov, D.A.2    Mironov, A.A.3    Gelfand, M.S.4
  • 56
    • 35048832520 scopus 로고    scopus 로고
    • Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum
    • Vogl, C., Grill, S., Schilling, O., Stülke, J., Mack, M., and Stolz, J. (2007). Characterization of riboflavin (vitamin B2) transport proteins from Bacillus subtilis and Corynebacterium glutamicum. J. Bacteriol. 189, 7367-7375.
    • (2007) J. Bacteriol. , vol.189 , pp. 7367-7375
    • Vogl, C.1    Grill, S.2    Schilling, O.3    Stülke, J.4    MacK, M.5    Stolz, J.6
  • 57
    • 84875195134 scopus 로고    scopus 로고
    • Novel riboflavin transporter family RFVT/SLC52: Identification, nomenclature, functional characterization and genetic diseases of RFVT/SLC52
    • Yonezawa, A. and Inui, K.-I. (2013). Novel riboflavin transporter family RFVT/SLC52: identification, nomenclature, functional characterization and genetic diseases of RFVT/SLC52. Mol. Aspects Med. 34, 693-701.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 693-701
    • Yonezawa, A.1    Inui, K.-I.2
  • 58
    • 84875191343 scopus 로고    scopus 로고
    • The human concentrative and equilibrative nucleoside transporter families, SLC28 and SLC29
    • Young, J.D., Yao, S.Y.M., Baldwin, J.M., Cass, C.E., and Baldwin, S.A. (2013). The human concentrative and equilibrative nucleoside transporter families, SLC28 and SLC29. Mol. Aspects Med. 34, 529-547.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 529-547
    • Young, J.D.1    Yao, S.Y.M.2    Baldwin, J.M.3    Cass, C.E.4    Baldwin, S.A.5
  • 59
    • 84875206514 scopus 로고    scopus 로고
    • Folate and thiamine transporters mediated by facilitative carriers (SLC19A1-3 and SLC46A1) and folate receptors
    • Zhao, R. and Goldman, I.D. (2013). Folate and thiamine transporters mediated by facilitative carriers (SLC19A1-3 and SLC46A1) and folate receptors. Mol. Aspects Med. 34, 373-385.
    • (2013) Mol. Aspects Med. , vol.34 , pp. 373-385
    • Zhao, R.1    Goldman, I.D.2
  • 60
    • 0026011268 scopus 로고
    • The nadI region of Salmonella typhimurium encodes a bifunctional regulatory protein
    • Zhu, N. and Roth, J.R. (1991). The nadI region of Salmonella typhimurium encodes a bifunctional regulatory protein. J. Bacteriol. 173, 1302-1310.
    • (1991) J. Bacteriol. , vol.173 , pp. 1302-1310
    • Zhu, N.1    Roth, J.R.2
  • 61
    • 0024720318 scopus 로고
    • Genetic characterization of the pnuC gene, which encodes a component of the nicotinamide mononucleotide transport system in Salmonella typhimurium
    • Zhu, N., Olivera, B.M., and Roth, J.R. (1989). Genetic characterization of the pnuC gene, which encodes a component of the nicotinamide mononucleotide transport system in Salmonella typhimurium. J. Bacteriol. 171, 4402-4409.
    • (1989) J. Bacteriol. , vol.171 , pp. 4402-4409
    • Zhu, N.1    Olivera, B.M.2    Roth, J.R.3
  • 62
    • 0026085518 scopus 로고
    • Activity of the nicotinamide mononucleotide transport system is regulated in Salmonella typhimurium
    • Zhu, N., Olivera, B.M., and Roth, J.R. (1991). Activity of the nicotinamide mononucleotide transport system is regulated in Salmonella typhimurium. J. Bacteriol. 173, 1311-1320.
    • (1991) J. Bacteriol. , vol.173 , pp. 1311-1320
    • Zhu, N.1    Olivera, B.M.2    Roth, J.R.3
  • 63
    • 0014093442 scopus 로고
    • Enzymatic joining of DNA strands: A novel reaction of diphosphopyridine nucleotide
    • Zimmerman, S.B., Little, J.W., Oshinsky, C.K., and Gellert, M. (1967). Enzymatic joining of DNA strands: a novel reaction of diphosphopyridine nucleotide. Proc. Natl. Acad. Sci. USA 57, 1841-1848.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.57 , pp. 1841-1848
    • Zimmerman, S.B.1    Little, J.W.2    Oshinsky, C.K.3    Gellert, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.