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Volumn 6, Issue 7, 2011, Pages

E. coli Histidine triad nucleotide binding protein 1 (echint) is a catalytic regulator of d-alanine dehydrogenase (dada) activity in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALANINE DEHYDROGENASE; CARBON; DEXTRO AMINO ACID OXIDASE; HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN 1; NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; ACID ANHYDRIDE HYDROLASE; ESCHERICHIA COLI PROTEIN; GUANOSINE PHOSPHATE; HISTIDINE TRIAD PROTEIN, E COLI;

EID: 79959976719     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020897     Document Type: Article
Times cited : (13)

References (34)
  • 1
    • 0032883882 scopus 로고    scopus 로고
    • The histidine triad superfamily of nucleotide-binding proteins
    • Brenner C, Bieganowski P, Pace H, Huebner K, (1999) The histidine triad superfamily of nucleotide-binding proteins. J Cell Physiol 181: 179-187.
    • (1999) J Cell Physiol , vol.181 , pp. 179-187
    • Brenner, C.1    Bieganowski, P.2    Pace, H.3    Huebner, K.4
  • 2
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • Brenner C, (2002) Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 41: 9003-9014.
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 3
    • 0034634523 scopus 로고    scopus 로고
    • Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins
    • Korsisaari N, Makela TP, (2000) Interactions of Cdk7 and Kin28 with Hint/PKCI-1 and Hnt1 histidine triad proteins. J Biol Chem 275: 34837-34840.
    • (2000) J Biol Chem , vol.275 , pp. 34837-34840
    • Korsisaari, N.1    Makela, T.P.2
  • 4
    • 0038245322 scopus 로고    scopus 로고
    • The histidine triad protein Hint is not required for murine development or Cdk7 function
    • Korsisaari N, Rossi DJ, Luukko K, Huebner K, Henkemeyer M, et al. (2003) The histidine triad protein Hint is not required for murine development or Cdk7 function. Mol Cell Biol 23: 3929-3935.
    • (2003) Mol Cell Biol , vol.23 , pp. 3929-3935
    • Korsisaari, N.1    Rossi, D.J.2    Luukko, K.3    Huebner, K.4    Henkemeyer, M.5
  • 5
    • 23844441846 scopus 로고    scopus 로고
    • The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-beta-catenin-mediated transcription
    • Weiske J, Huber O, (2005) The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-beta-catenin-mediated transcription. J Cell Sci 118: 3117-3129.
    • (2005) J Cell Sci , vol.118 , pp. 3117-3129
    • Weiske, J.1    Huber, O.2
  • 6
    • 32244448801 scopus 로고    scopus 로고
    • Hint1 is a haplo-insufficient tumor suppressor in mice
    • Li H, Zhang Y, Su T, Santella RM, Weinstein IB, (2006) Hint1 is a haplo-insufficient tumor suppressor in mice. Oncogene 25: 713-721.
    • (2006) Oncogene , vol.25 , pp. 713-721
    • Li, H.1    Zhang, Y.2    Su, T.3    Santella, R.M.4    Weinstein, I.B.5
  • 7
    • 3142770404 scopus 로고    scopus 로고
    • Aberrant gene expression in human non small cell lung carcinoma cells exposed to demethylating agent 5-aza-2′-deoxycytidine
    • Yuan BZ, Jefferson AM, Popescu NC, Reynolds SH, (2004) Aberrant gene expression in human non small cell lung carcinoma cells exposed to demethylating agent 5-aza-2′-deoxycytidine. Neoplasia 6: 412-429.
    • (2004) Neoplasia , vol.6 , pp. 412-429
    • Yuan, B.Z.1    Jefferson, A.M.2    Popescu, N.C.3    Reynolds, S.H.4
  • 8
    • 68549111325 scopus 로고    scopus 로고
    • Identifying apoptosis-evasion proteins/pathways in human hepatoma cells via induction of cellular hormesis by UV irradiation
    • Hsieh SY, Hsu CY, He JR, Liu CL, Lo SJ, et al. (2009) Identifying apoptosis-evasion proteins/pathways in human hepatoma cells via induction of cellular hormesis by UV irradiation. J Proteome Res 8: 3977-3986.
    • (2009) J Proteome Res , vol.8 , pp. 3977-3986
    • Hsieh, S.Y.1    Hsu, C.Y.2    He, J.R.3    Liu, C.L.4    Lo, S.J.5
  • 9
    • 78751549680 scopus 로고    scopus 로고
    • Ablation of the tumor suppressor histidine triad nucleotide binding protein 1 is protective against hepatic ischemia/reperfusion injury
    • Martin J, Romanque P, Maurhofer O, Schmitter K, Ferrand G, et al. (2011) Ablation of the tumor suppressor histidine triad nucleotide binding protein 1 is protective against hepatic ischemia/reperfusion injury. Hepatology 53: 243-52.
    • (2011) Hepatology , vol.53 , pp. 243-252
    • Martin, J.1    Romanque, P.2    Maurhofer, O.3    Schmitter, K.4    Ferrand, G.5
  • 10
    • 0037934419 scopus 로고    scopus 로고
    • Deletion of histidine triad nucleotide-binding protein 1/PKC-interacting protein in mice enhances cell growth and carcinogenesis
    • Su T, Suzui M, Wang L, Lin CS, Xing WQ, et al. (2003) Deletion of histidine triad nucleotide-binding protein 1/PKC-interacting protein in mice enhances cell growth and carcinogenesis. Proc Natl Acad Sci USA 100: 7824-7829.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7824-7829
    • Su, T.1    Suzui, M.2    Wang, L.3    Lin, C.S.4    Xing, W.Q.5
  • 11
    • 33947523522 scopus 로고    scopus 로고
    • Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins
    • Chou T-F, Wagner CR, (2007) Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins. J Biol Chem 282: 4719-4727.
    • (2007) J Biol Chem , vol.282 , pp. 4719-4727
    • Chou, T.-F.1    Wagner, C.R.2
  • 12
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-537.
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrin-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5
  • 13
    • 12344264078 scopus 로고    scopus 로고
    • P80, the HinT interacting membrane protein, is a secreted antigen of Mycoplasma hominis
    • Hopfe M, Hoffmann R, Henrich B, (2004) P80, the HinT interacting membrane protein, is a secreted antigen of Mycoplasma hominis. BMC Microbiol 4: 46.
    • (2004) BMC Microbiol , vol.4 , pp. 46
    • Hopfe, M.1    Hoffmann, R.2    Henrich, B.3
  • 14
    • 0034933581 scopus 로고    scopus 로고
    • The cytosolic HinT protein of Mycoplasma hominis interacts with two membrane proteins
    • Kitzerow A, Henrich B, (2001) The cytosolic HinT protein of Mycoplasma hominis interacts with two membrane proteins. Mol Microbiol 41: 279-287.
    • (2001) Mol Microbiol , vol.41 , pp. 279-287
    • Kitzerow, A.1    Henrich, B.2
  • 15
    • 0037192795 scopus 로고    scopus 로고
    • Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3
    • Bieganowski P, Garrison PN, Hodawadekar SC, Faye G, Barnes LD, et al. (2002) Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3. J Biol Chem 277: 10852-10860.
    • (2002) J Biol Chem , vol.277 , pp. 10852-10860
    • Bieganowski, P.1    Garrison, P.N.2    Hodawadekar, S.C.3    Faye, G.4    Barnes, L.D.5
  • 16
    • 0029980110 scopus 로고    scopus 로고
    • Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins
    • Lima CD, Klein MG, Weinstein IB, Hendrickson WA, (1996) Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. Proc Natl Acad Sci USA 93: 5357-5362.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5357-5362
    • Lima, C.D.1    Klein, M.G.2    Weinstein, I.B.3    Hendrickson, W.A.4
  • 17
    • 78549261685 scopus 로고    scopus 로고
    • Probing the impact of the echinT C-terminal domain on structure and catalysis
    • Bardaweel S, Pace J, Chou T-F, Cody V, Wagner CR, (2010) Probing the impact of the echinT C-terminal domain on structure and catalysis. J Mol Biol 404: 627-638.
    • (2010) J Mol Biol , vol.404 , pp. 627-638
    • Bardaweel, S.1    Pace, J.2    Chou, T.-F.3    Cody, V.4    Wagner, C.R.5
  • 18
    • 36049048984 scopus 로고    scopus 로고
    • Impact of the C-terminal loop of histidine triad nucleotide binding protein1 (Hint1) on substrate specificity
    • Chou T-F, Sham Y, Wagner CR, (2007) Impact of the C-terminal loop of histidine triad nucleotide binding protein1 (Hint1) on substrate specificity. Biochemistry 46: 13074-13079.
    • (2007) Biochemistry , vol.46 , pp. 13074-13079
    • Chou, T.-F.1    Sham, Y.2    Wagner, C.R.3
  • 19
    • 24044464543 scopus 로고    scopus 로고
    • Functional analysis of 1440 Escherichia coli genes using the combination of knock-out library and phenotype microarrays
    • Ito M, Baba T, Morib H, Mori H, (2005) Functional analysis of 1440 Escherichia coli genes using the combination of knock-out library and phenotype microarrays. Metab Engineering 7: 318-327.
    • (2005) Metab Engineering , vol.7 , pp. 318-327
    • Ito, M.1    Baba, T.2    Morib, H.3    Mori, H.4
  • 20
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection
    • Baba T, Aral T, Hasegewal M, Takail Y, Okumural Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection. Mol Systems Biol 2: 1-11.
    • (2006) Mol Systems Biol , vol.2 , pp. 1-11
    • Baba, T.1    Aral, T.2    Hasegewal, M.3    Takail, Y.4    Okumural, Y.5
  • 21
    • 0034911878 scopus 로고    scopus 로고
    • Phenotype microarrays for high-throughput phenotypic testing and assay of gene function
    • Bochner BR, Gadzinski P, Panomitros E, (2001) Phenotype microarrays for high-throughput phenotypic testing and assay of gene function. Genome Res 11: 1246-1255.
    • (2001) Genome Res , vol.11 , pp. 1246-1255
    • Bochner, B.R.1    Gadzinski, P.2    Panomitros, E.3
  • 22
    • 0004136246 scopus 로고
    • 2nd Ed. N.Y., Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, ISBN 0-87969-309-6
    • Sambrook J, Fritsch EF, Maniatis T, (1989) Molecular Cloning: a laboratory manual. 2nd ed. N.Y., Cold Spring Harbor Laboratory Cold Spring Harbor Laboratory Press ISBN 0-87969-309-6.
    • (1989) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 23
    • 34247380394 scopus 로고    scopus 로고
    • Phosphoramidate pronucleotides: A comparison of the phosphoramidase substrate specificity of human and E. coli histidine triad nucleotide binding proteins (Hint1)
    • Chou T-F, Baraniak J, Kaczmarek R, Zhou X, Cheng J, et al. (2007) Phosphoramidate pronucleotides: A comparison of the phosphoramidase substrate specificity of human and E. coli histidine triad nucleotide binding proteins (Hint1). Mol Pharmaceutics 4: 208-217.
    • (2007) Mol Pharmaceutics , vol.4 , pp. 208-217
    • Chou, T.-F.1    Baraniak, J.2    Kaczmarek, R.3    Zhou, X.4    Cheng, J.5
  • 24
    • 0017181918 scopus 로고
    • Biochemical, genetic, and regulatory studies of alanine catabolism in Escherichia coli K12
    • Franklin F, Venables W, (1976) Biochemical, genetic, and regulatory studies of alanine catabolism in Escherichia coli K12. Mol Gen Genet 149: 229-237.
    • (1976) Mol Gen Genet , vol.149 , pp. 229-237
    • Franklin, F.1    Venables, W.2
  • 25
    • 0021104415 scopus 로고
    • Proline Dehydrogenase from Escherichia coli K12, properties of the membrane associated enzyme
    • Abrahamson J, Baker L, Stephenson J, Wood J, (1983) Proline Dehydrogenase from Escherichia coli K12, properties of the membrane associated enzyme. Eur J Biochem 134: 77-82.
    • (1983) Eur J Biochem , vol.134 , pp. 77-82
    • Abrahamson, J.1    Baker, L.2    Stephenson, J.3    Wood, J.4
  • 26
    • 17644385585 scopus 로고    scopus 로고
    • 31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions
    • Chou T-F, Bieganowski P, Shilinski K, Cheng J, Brenner C, et al. (2005) 31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions. J Bio Chem 280: 15356-15361.
    • (2005) J Bio Chem , vol.280 , pp. 15356-15361
    • Chou, T.-F.1    Bieganowski, P.2    Shilinski, K.3    Cheng, J.4    Brenner, C.5
  • 27
    • 0018821298 scopus 로고
    • Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli
    • Olsiewski PJ, Kaczorowski GJ, Walsh C, (1980) Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli. J Biol Chem 255: 4487-4494.
    • (1980) J Biol Chem , vol.255 , pp. 4487-4494
    • Olsiewski, P.J.1    Kaczorowski, G.J.2    Walsh, C.3
  • 29
    • 0015836721 scopus 로고
    • D-alanine oxidase from Escherichia coli: localization and induction by Lalanine
    • Raunio RP, Jenkins WT, (1973) D-alanine oxidase from Escherichia coli: localization and induction by Lalanine. J Bacteriol 115: 560-566.
    • (1973) J Bacteriol , vol.115 , pp. 560-566
    • Raunio, R.P.1    Jenkins, W.T.2
  • 30
    • 4444368953 scopus 로고    scopus 로고
    • Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-alanine dehydrogenase from Escherichia coli
    • Deutch CE, (2004) Oxidation of 3,4-dehydro-D-proline and other D-amino acid analogues by D-alanine dehydrogenase from Escherichia coli. FEMS Microbiol Lett 238: 383-389.
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 383-389
    • Deutch, C.E.1
  • 31
    • 0028294870 scopus 로고
    • Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase
    • Lobocka M, Hennig J, Wild J, Klopotowski T, (1994) Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase. J Bacteriol 176: 1500-1510.
    • (1994) J Bacteriol , vol.176 , pp. 1500-1510
    • Lobocka, M.1    Hennig, J.2    Wild, J.3    Klopotowski, T.4
  • 32
    • 0021824417 scopus 로고
    • Germination-initiation and inhibitory activities of L- and D-alanine analogues for Bacillus subtilis spores, Modification of methyl group of L and D-alanine
    • Yasuda Y, Tochikubo K, (1985) Germination-initiation and inhibitory activities of L- and D-alanine analogues for Bacillus subtilis spores, Modification of methyl group of L and D-alanine. Microbiol Immunol 29: 229-241.
    • (1985) Microbiol Immunol , vol.29 , pp. 229-241
    • Yasuda, Y.1    Tochikubo, K.2
  • 33
    • 0024561489 scopus 로고
    • Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly
    • Walsh CT, (1989) Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly. J Biol Chem 264: 2393-2396.
    • (1989) J Biol Chem , vol.264 , pp. 2393-2396
    • Walsh, C.T.1


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