메뉴 건너뛰기




Volumn 288, Issue 52, 2013, Pages 36827-36840

Functional identification of the hypoxanthine/guanine transporters YjcD and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI K-12; FUNCTIONAL IDENTIFICATION; GENES ENCODE; HIGH AFFINITY; STRUCTURE FUNCTIONS; TRANSPORTER GENES;

EID: 84891472551     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.523340     Document Type: Article
Times cited : (38)

References (40)
  • 3
    • 77949877904 scopus 로고    scopus 로고
    • Identification and functional characterization of the first nucleobase transporter in mammals: Implication in the species difference in the intestinal absorption mechanism of nucleobases and their analogs between higher primates and other mammals
    • Yamamoto, S., Inoue, K., Murata, T., Kamigaso, S., Yasujima, T., Maeda J. Y., Yoshida, Y., Ohta, K. Y., and Yuasa, H. (2010) Identification and functional characterization of the first nucleobase transporter in mammals: implication in the species difference in the intestinal absorption mechanism of nucleobases and their analogs between higher primates and other mammals. J. Biol. Chem. 285, 6522-6531
    • (2010) J. Biol. Chem. , vol.285 , pp. 6522-6531
    • Yamamoto, S.1    Inoue, K.2    Murata, T.3    Kamigaso, S.4    Yasujima, T.5    Maeda, J.Y.6    Yoshida, Y.7    Ohta, K.Y.8    Yuasa, H.9
  • 5
    • 77953472186 scopus 로고    scopus 로고
    • Nucleoside/nucleobase transporters: Drug targets of the future?
    • Köse, M., and Schiedel, A. C. (2009) Nucleoside/nucleobase transporters: drug targets of the future? Future Med. Chem. 1, 303-326
    • (2009) Future Med. Chem. , vol.1 , pp. 303-326
    • Köse, M.1    Schiedel, A.C.2
  • 6
    • 84867547605 scopus 로고    scopus 로고
    • Insights to the evolution of nucleobase-ascorbate transporters (NAT/NCS2) from the Cys-scanning analysis of xanthine permease XanQ
    • Frillingos, S. (2012) Insights to the evolution of nucleobase-ascorbate transporters (NAT/NCS2) from the Cys-scanning analysis of xanthine permease XanQ. Int. J. Biochem. Mol. Biol. 3, 250-272
    • (2012) Int. J. Biochem. Mol. Biol. , vol.3 , pp. 250-272
    • Frillingos, S.1
  • 7
    • 84860862465 scopus 로고    scopus 로고
    • Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli
    • Papakostas, K., and Frillingos, S. (2012) Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli. J. Biol. Chem. 287, 15684-15695
    • (2012) J. Biol. Chem. , vol.287 , pp. 15684-15695
    • Papakostas, K.1    Frillingos, S.2
  • 8
    • 84864353522 scopus 로고    scopus 로고
    • Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family
    • Kosti, V., Lambrinidis, G., Myrianthopoulos, V., Diallinas, G., and Mikros, E. (2012) Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family. PLoS One 7, e41939
    • (2012) PLoS One , vol.7
    • Kosti, V.1    Lambrinidis, G.2    Myrianthopoulos, V.3    Diallinas, G.4    Mikros, E.5
  • 9
    • 0026568864 scopus 로고
    • Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase
    • Danielsen, S., Kilstrup, M., Barilla, K., Jochimsen, B., and Neuhard, J. (1992) Characterization of the Escherichia coli codBA operon encoding cytosine permease and cytosine deaminase. Mol. Microbiol. 6, 1335-1344
    • (1992) Mol. Microbiol. , vol.6 , pp. 1335-1344
    • Danielsen, S.1    Kilstrup, M.2    Barilla, K.3    Jochimsen, B.4    Neuhard, J.5
  • 10
    • 0032762639 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
    • Cusa, E., Obradors, N., Baldomà, L., Badía, J., and Aguilar, J. (1999) Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J. Bacteriol. 181, 7479-7484
    • (1999) J. Bacteriol. , vol.181 , pp. 7479-7484
    • Cusa, E.1    Obradors, N.2    Baldomà, L.3    Badía, J.4    Aguilar, J.5
  • 11
    • 0028931056 scopus 로고
    • Uracil uptake in Escherichia coli K-12: Isolation of uraA mutants and cloning of the gene
    • Andersen, P. S., Frees, D., Fast R., and Mygind, B. (1995) Uracil uptake in Escherichia coli K-12: isolation of uraA mutants and cloning of the gene. J. Bacteriol. 177, 2008-2013
    • (1995) J. Bacteriol. , vol.177 , pp. 2008-2013
    • Andersen, P.S.1    Frees, D.2    Fast, R.3    Mygind, B.4
  • 12
    • 20444463884 scopus 로고    scopus 로고
    • Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli
    • Karatza, P., and Frillingos, S. (2005) Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli. Mol. Membr. Biol. 22, 251-261
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 251-261
    • Karatza, P.1    Frillingos, S.2
  • 13
    • 0942276403 scopus 로고    scopus 로고
    • The AzgA purine transporter of aspergillus nidulans: Characterization of a protein belonging to a new phylogenetic cluster
    • Cecchetto, G., Amillis, S., Diallinas, G., Scazzocchio, C., and Drevet, C. (2004) The AzgA purine transporter of Aspergillus nidulans: characterization of a protein belonging to a new phylogenetic cluster. J. Biol. Chem. 279, 3132-3141
    • (2004) J. Biol. Chem. , vol.279 , pp. 3132-3141
    • Cecchetto, G.1    Amillis, S.2    Diallinas, G.3    Scazzocchio, C.4    Drevet, C.5
  • 14
    • 58149527702 scopus 로고    scopus 로고
    • AtAzgA1 and AtAzgA2 comprise a novel family of purine transporters in Arabidopsis
    • Mansfield, T. A., Schultes, N. P., and Mourad, G. S. (2009) AtAzgA1 and AtAzgA2 comprise a novel family of purine transporters in Arabidopsis. FEBS Lett. 583, 481-486
    • (2009) FEBS Lett. , vol.583 , pp. 481-486
    • Mansfield, T.A.1    Schultes, N.P.2    Mourad, G.S.3
  • 15
    • 0021070153 scopus 로고
    • Transport of nucleic acid bases into Escherichia coli
    • Burton, K. (1983) Transport of nucleic acid bases into Escherichia coli. J. Gen. Microbiol. 129, 3505-3513
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 3505-3513
    • Burton, K.1
  • 16
    • 0028045064 scopus 로고
    • Adenine transport in Escherichia coli
    • Burton, K. (1994) Adenine transport in Escherichia coli. Proc. Biol. Sci. 255, 153-157
    • (1994) Proc. Biol. Sci. , vol.255 , pp. 153-157
    • Burton, K.1
  • 18
    • 33845966781 scopus 로고    scopus 로고
    • Cysteinescanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential and Ile-329-Val-339 form an α-helix
    • Karatza, P., Panos, P., Georgopoulou, E., and Frillingos, S. (2006) Cysteinescanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential and Ile-329-Val-339 form an α-helix. J. Biol. Chem. 281, 39881-39890
    • (2006) J. Biol. Chem. , vol.281 , pp. 39881-39890
    • Karatza, P.1    Panos, P.2    Georgopoulou, E.3    Frillingos, S.4
  • 19
    • 46649112362 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: Ile-432 and Asn-430 are important
    • Papakostas, K., Georgopoulou, E., and Frillingos, S. (2008) Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: Ile-432 and Asn-430 are important. J. Biol. Chem. 283, 13666-13678
    • (2008) J. Biol. Chem. , vol.283 , pp. 13666-13678
    • Papakostas, K.1    Georgopoulou, E.2    Frillingos, S.3
  • 20
    • 69949131591 scopus 로고    scopus 로고
    • Role of intramembrane polar residues in the YgfO xanthine permease: His-31 and Asn-93 are crucial for affinity and specificity, and Asp-304 and Glu-272 are irreplaceable
    • Karena, E., and Frillingos, S. (2009) Role of intramembrane polar residues in the YgfO xanthine permease: His-31 and Asn-93 are crucial for affinity and specificity, and Asp-304 and Glu-272 are irreplaceable. J. Biol. Chem. 284, 24257-24268
    • (2009) J. Biol. Chem. , vol.284 , pp. 24257-24268
    • Karena, E.1    Frillingos, S.2
  • 21
    • 77953482526 scopus 로고    scopus 로고
    • Purine substrate recognition by the nucleobase-ascorbate transporter motif in the YgfO xanthine permease: Asn-325 binds and Ala-323 senses substrate
    • Georgopoulou, E., Mermelekas, G., Karena, E., and Frillingos, S. (2010) Purine substrate recognition by the nucleobase-ascorbate transporter motif in the YgfO xanthine permease: Asn-325 binds and Ala-323 senses substrate. J. Biol. Chem. 285, 19422-19433
    • (2010) J. Biol. Chem. , vol.285 , pp. 19422-19433
    • Georgopoulou, E.1    Mermelekas, G.2    Karena, E.3    Frillingos, S.4
  • 22
    • 78049395093 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of helices TM8, TM9a, TM9b and intervening loops in the YgfO xanthine permease: A carboxyl group is essential at position Asp-276
    • Mermelekas, G., Georgopoulou, E., Kallis, A., Botou M., Vlantos, V., and Frillingos, S. (2010) Cysteine-scanning analysis of helices TM8, TM9a, TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at position Asp-276. J. Biol. Chem. 285, 35011-35020
    • (2010) J. Biol. Chem. , vol.285 , pp. 35011-35020
    • Mermelekas, G.1    Georgopoulou, E.2    Kallis, A.3    Botou, M.4    Vlantos, V.5    Frillingos, S.6
  • 23
    • 80655144745 scopus 로고    scopus 로고
    • The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli
    • Karena, E., and Frillingos, S. (2011) The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli. J. Biol. Chem. 286, 39595-39605
    • (2011) J. Biol. Chem. , vol.286 , pp. 39595-39605
    • Karena, E.1    Frillingos, S.2
  • 24
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., Nojima, H., and Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96, 23-28
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 25
    • 0018850485 scopus 로고
    • Lactose carrier protein of Escherichia coli: Construction and expression of plasmids carrying the y gene of the lac operon
    • Teather, R. M., Bramhall, J., Riede, I., Wright, J. K., Fürst, M., Aichele, G., Wilhelm, U., and Overath, P. (1980) Lactose carrier protein of Escherichia coli: construction and expression of plasmids carrying the Y gene of the lac operon. Eur. J. Biochem. 108, 223-231
    • (1980) Eur. J. Biochem. , vol.108 , pp. 223-231
    • Teather, R.M.1    Bramhall, J.2    Riede, I.3    Wright, J.K.4    Fürst, M.5    Aichele, G.6    Wilhelm, U.7    Overath, P.8
  • 27
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap-extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap-extension using the polymerase chain reaction. Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 28
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., Biegert, A., and Lupas, A. N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248
    • (2005) Nucleic Acids Res. , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 30
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 31
    • 24044436844 scopus 로고    scopus 로고
    • Experimentally constrained topology models for 51,208 bacterial inner membrane proteins
    • Granseth, E., Daley, D. O., Rapp, M., Melén, K., and von Heijne, G. (2005) Experimentally constrained topology models for 51,208 bacterial inner membrane proteins. J. Mol. Biol. 352, 489-494
    • (2005) J. Mol. Biol. , vol.352 , pp. 489-494
    • Granseth, E.1    Daley, D.O.2    Rapp, M.3    Melén, K.4    Von Heijne, G.5
  • 32
    • 0042622380 scopus 로고    scopus 로고
    • SWISSMODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISSMODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 33
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 27-28
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38, 27-28
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 34
    • 0016701087 scopus 로고
    • Transport of purines and deoxyadenosine in Escherichia coli
    • Roy-Burman, S., and Visser, D. W. (1975) Transport of purines and deoxyadenosine in Escherichia coli. J. Biol. Chem. 250, 9270-9275
    • (1975) J. Biol. Chem. , vol.250 , pp. 9270-9275
    • Roy-Burman, S.1    Visser, D.W.2
  • 35
    • 84891417389 scopus 로고    scopus 로고
    • A critical role for the putative NCS2 nucleobase permease YjcD in the sensitivity of Escherichia coli to cytotoxic and mutagenic purine analogs
    • Kozmin, S. G., Stepchenkova, E. I., Chow, S. C., and Schaaper, R. M. (2013) A critical role for the putative NCS2 nucleobase permease YjcD in the sensitivity of Escherichia coli to cytotoxic and mutagenic purine analogs. MBio 4, e00661-13
    • (2013) MBio , vol.4
    • Kozmin, S.G.1    Stepchenkova, E.I.2    Chow, S.C.3    Schaaper, R.M.4
  • 38
    • 20444448199 scopus 로고    scopus 로고
    • The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway
    • Koukaki, M., Vlanti, A., Goudela, S., Pantazopoulou, A., Gioule, H., Tournaviti, S., and Diallinas, G. (2005) The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway. J. Mol. Biol. 350, 499-513
    • (2005) J. Mol. Biol. , vol.350 , pp. 499-513
    • Koukaki, M.1    Vlanti, A.2    Goudela, S.3    Pantazopoulou, A.4    Gioule, H.5    Tournaviti, S.6    Diallinas, G.7
  • 39
    • 79960915923 scopus 로고    scopus 로고
    • Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter
    • Amillis, S., Kosti, V., Pantazopoulou, A., Mikros, E., and Diallinas, G. (2011) Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter. J. Mol. Biol. 411, 567-580
    • (2011) J. Mol. Biol. , vol.411 , pp. 567-580
    • Amillis, S.1    Kosti, V.2    Pantazopoulou, A.3    Mikros, E.4    Diallinas, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.