메뉴 건너뛰기




Volumn 192, Issue 19, 2010, Pages 4821-4826

Properties of the NAC (nitrogen assimilation control protein)-binding site within the ureD promoter of Klebsiella pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NITROGEN ASSIMILATION CONTROL PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG; TRANSCRIPTION FACTOR; URED PROTEIN, BACTERIA;

EID: 77957340312     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00883-09     Document Type: Article
Times cited : (7)

References (30)
  • 1
    • 0031935121 scopus 로고    scopus 로고
    • Genetic analysis, using P22 challenge phage, of the nitrogen activator protein DNA-binding site in the Klebsiella aerogenes put operon
    • Chen, L. M., T. J. Goss, R. A. Bender, S. Swift, and S. Maloy. 1998. Genetic analysis, using P22 challenge phage, of the nitrogen activator protein DNA-binding site in the Klebsiella aerogenes put operon. J. Bacteriol. 180:571-577.
    • (1998) J. Bacteriol. , vol.180 , pp. 571-577
    • Chen, L.M.1    Goss, T.J.2    Bender, R.A.3    Swift, S.4    Maloy, S.5
  • 2
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 3
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., T. L. Steck, and D. F. Wallach. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 4
    • 77957366332 scopus 로고    scopus 로고
    • Expanded role for the nitrogen assimilation control protein in the response of Klebsiella pneumoniae to nitrogen stress
    • Frisch, R. L., and R. A. Bender. 2010. Expanded role for the nitrogen assimilation control protein in the response of Klebsiella pneumoniae to nitrogen stress. J. Bacteriol. 192:4812-4820.
    • (2010) J. Bacteriol. , vol.192 , pp. 4812-4820
    • Frisch, R.L.1    Bender, R.A.2
  • 5
    • 0016168742 scopus 로고
    • Direct selection for P1-sensitive mutants of enteric bacteria
    • Goldberg, R. B., R. A. Bender, and S. L. Streicher. 1974. Direct selection for P1-sensitive mutants of enteric bacteria. J. Bacteriol. 118:810-814.
    • (1974) J. Bacteriol. , vol.118 , pp. 810-814
    • Goldberg, R.B.1    Bender, R.A.2    Streicher, S.L.3
  • 6
    • 44949166755 scopus 로고    scopus 로고
    • The ArgP protein stimulates the Klebsiella pneumoniae gdhA promoter in a lysine-sensitive manner
    • Goss, T. J. 2008. The ArgP protein stimulates the Klebsiella pneumoniae gdhA promoter in a lysine-sensitive manner. J. Bacteriol. 190:4351-4359.
    • (2008) J. Bacteriol. , vol.190 , pp. 4351-4359
    • Goss, T.J.1
  • 7
    • 0029077341 scopus 로고
    • The nitrogen assimilation control protein, NAC, is a DNA binding transcription activator in Klebsiella aerogenes
    • Goss, T. J., and R. A. Bender. 1995. The nitrogen assimilation control protein, NAC, is a DNA binding transcription activator in Klebsiella aerogenes. J. Bacteriol. 177:3546-3555.
    • (1995) J. Bacteriol. , vol.177 , pp. 3546-3555
    • Goss, T.J.1    Bender, R.A.2
  • 8
    • 0031936277 scopus 로고    scopus 로고
    • Alanine catabolism in Klebsiella aerogenes: Molecular characterization of the dadAB operon and its regulation by the nitrogen assimilation control protein
    • Janes, B. K., and R. A. Bender. 1998. Alanine catabolism in Klebsiella aerogenes: molecular characterization of the dadAB operon and its regulation by the nitrogen assimilation control protein. J. Bacteriol. 180:563-570.
    • (1998) J. Bacteriol. , vol.180 , pp. 563-570
    • Janes, B.K.1    Bender, R.A.2
  • 9
    • 35648929353 scopus 로고    scopus 로고
    • Complex regulation of urease formation from the two promoters of the ure operon of Klebsiella pneumoniae
    • Liu, Q., and R. A. Bender. 2007. Complex regulation of urease formation from the two promoters of the ure operon of Klebsiella pneumoniae. J. Bacteriol. 189:7593-7599.
    • (2007) J. Bacteriol. , vol.189 , pp. 7593-7599
    • Liu, Q.1    Bender, R.A.2
  • 10
    • 3843122191 scopus 로고    scopus 로고
    • Identification of activating region (AR) of Escherichia coli LysR-type transcription factor CysB and CysB contact site on RNA polymerase alpha subunit at the cysP promoter
    • Lochowska, A., R. Iwanicka-Nowicka, J. Zaim, M. Witkowska-Zimny, K. Bolewska, and M. M. Hryniewicz. 2004. Identification of activating region (AR) of Escherichia coli LysR-type transcription factor CysB and CysB contact site on RNA polymerase alpha subunit at the cysP promoter. Mol. Microbiol. 53:791-806.
    • (2004) Mol. Microbiol. , vol.53 , pp. 791-806
    • Lochowska, A.1    Iwanicka-Nowicka, R.2    Zaim, J.3    Witkowska-Zimny, M.4    Bolewska, K.5    Hryniewicz, M.M.6
  • 12
    • 0025678940 scopus 로고
    • Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes
    • Macaluso, A., E. A. Best, and R. A. Bender. 1990. Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes. J. Bacteriol. 172:7249-7255.
    • (1990) J. Bacteriol. , vol.172 , pp. 7249-7255
    • Macaluso, A.1    Best, E.A.2    Bender, R.A.3
  • 14
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks, S. E., and P. C. Oyston. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154:3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 17
    • 0344406163 scopus 로고    scopus 로고
    • Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: Unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
    • Muraoka, S., R. Okumura, N. Ogawa, T. Nonaka, K. Miyashita, and T. Senda. 2003. Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J. Mol. Biol. 328:555-566.
    • (2003) J. Mol. Biol. , vol.328 , pp. 555-566
    • Muraoka, S.1    Okumura, R.2    Ogawa, N.3    Nonaka, T.4    Miyashita, K.5    Senda, T.6
  • 19
    • 0037407903 scopus 로고    scopus 로고
    • Nitrogen regulation of the codBA (cytosine deaminase) operon from Escherichia coli by the nitrogen assimilation control protein, NAC
    • Muse, W. B., C. J. Rosario, and R. A. Bender. 2003. Nitrogen regulation of the codBA (cytosine deaminase) operon from Escherichia coli by the nitrogen assimilation control protein, NAC. J. Bacteriol. 185:2920-2926.
    • (2003) J. Bacteriol. , vol.185 , pp. 2920-2926
    • Muse, W.B.1    Rosario, C.J.2    Bender, R.A.3
  • 20
    • 0029081139 scopus 로고
    • Activation of the Escherichia coli lacZ promoter by the Klebsiella aerogenes nitrogen assimilation control protein (NAC), a LysR family transcription factor
    • Pomposiello, P. J., and R. A. Bender. 1995. Activation of the Escherichia coli lacZ promoter by the Klebsiella aerogenes nitrogen assimilation control protein (NAC), a LysR family transcription factor. J. Bacteriol. 177:4820-4824.
    • (1995) J. Bacteriol. , vol.177 , pp. 4820-4824
    • Pomposiello, P.J.1    Bender, R.A.2
  • 21
    • 0031888239 scopus 로고    scopus 로고
    • Two roles for the DNA recognition site of the Klebsiella aerogenes nitrogen assimilation control protein
    • Pomposiello, P. J., B. K. Janes, and R. A. Bender. 1998. Two roles for the DNA recognition site of the Klebsiella aerogenes nitrogen assimilation control protein. J. Bacteriol. 180:578-585.
    • (1998) J. Bacteriol. , vol.180 , pp. 578-585
    • Pomposiello, P.J.1    Janes, B.K.2    Bender, R.A.3
  • 22
    • 77957360781 scopus 로고    scopus 로고
    • The LysR-type nitrogen assimilation control protein forms complexes with both long and short DNA binding sites in the absence of coeffectors
    • Rosario, C. J., R. L. Frisch, and R. A. Bender. 2010. The LysR-type nitrogen assimilation control protein forms complexes with both long and short DNA binding sites in the absence of coeffectors. J. Bacteriol. 192:4827-4833.
    • (2010) J. Bacteriol. , vol.192 , pp. 4827-4833
    • Rosario, C.J.1    Frisch, R.L.2    Bender, R.A.3
  • 23
    • 77957374566 scopus 로고    scopus 로고
    • Genetic analysis of the nitrogen assimilation control protein from Klebsiella pneumoniae
    • Rosario, C. J., B. K. Janes, and R. A. Bender. 2010. Genetic analysis of the nitrogen assimilation control protein from Klebsiella pneumoniae. J. Bacteriol. 192:4834-4846.
    • (2010) J. Bacteriol. , vol.192 , pp. 4834-4846
    • Rosario, C.J.1    Janes, B.K.2    Bender, R.A.3
  • 24
    • 28844443806 scopus 로고    scopus 로고
    • Importance of tetramer formation by the nitrogen assimilation control protein for strong repression of glutamate dehydrogenase formation in Klebsiella pneumoniae
    • Rosario, C. J., and R. A. Bender. 2005. Importance of tetramer formation by the nitrogen assimilation control protein for strong repression of glutamate dehydrogenase formation in Klebsiella pneumoniae. J. Bacteriol. 187:8291-8299.
    • (2005) J. Bacteriol. , vol.187 , pp. 8291-8299
    • Rosario, C.J.1    Bender, R.A.2
  • 25
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 26
    • 0027406501 scopus 로고
    • The product of the Klebsiella aerogenes nac (nitrogen assimilation control) gene is sufficient for activation of the hut operons and repression of the gdh operon
    • Schwacha, A., and R. A. Bender. 1993. The product of the Klebsiella aerogenes nac (nitrogen assimilation control) gene is sufficient for activation of the hut operons and repression of the gdh operon. J. Bacteriol. 175:2116-2124.
    • (1993) J. Bacteriol. , vol.175 , pp. 2116-2124
    • Schwacha, A.1    Bender, R.A.2
  • 27
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53:85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 28
    • 0029926274 scopus 로고    scopus 로고
    • Positive selection vectors for allelic exchange
    • Skorupski, K., and R. K. Taylor. 1996. Positive selection vectors for allelic exchange. Gene 169:47-52.
    • (1996) Gene , vol.169 , pp. 47-52
    • Skorupski, K.1    Taylor, R.K.2
  • 29
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E. L., S. R. Eddy, and R. Durbin. 1997. Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 28:405-420.
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 30
    • 0028809521 scopus 로고
    • Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase alpha subunit
    • Tao, K., C. Zou, N. Fujita, and A. Ishihama. 1995. Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase alpha subunit. J. Bacteriol. 177:6740-6744.
    • (1995) J. Bacteriol. , vol.177 , pp. 6740-6744
    • Tao, K.1    Zou, C.2    Fujita, N.3    Ishihama, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.