메뉴 건너뛰기




Volumn 187, Issue 15, 2005, Pages 5452-5459

Functional replacement of the oligomerization domain of H-NS by the Hha protein of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HHA PROTEIN; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; UNCLASSIFIED DRUG; YMO PROTEIN;

EID: 22644445062     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.15.5452-5459.2005     Document Type: Article
Times cited : (13)

References (42)
  • 2
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H. W., and D. Roulland-Dussoix. 1969. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 41:459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 3
    • 0032509098 scopus 로고    scopus 로고
    • Lac and λ repressors relieve silencing of the Escherichia coli bgl promoter. Activation by alteration of a repressing nucleoprotein complex
    • Caramel, A., and K. Schnetz. 1998. Lac and λ repressors relieve silencing of the Escherichia coli bgl promoter. Activation by alteration of a repressing nucleoprotein complex. J. Mol. Biol. 284:875-883.
    • (1998) J. Mol. Biol. , vol.284 , pp. 875-883
    • Caramel, A.1    Schnetz, K.2
  • 4
    • 0027185636 scopus 로고
    • Escherichia coli hha mutants, DNA supercoiling and expression of haemolysin genes from recombinant plasmid pANN202-312
    • Carmona, M., C. Balsalobre, F. J. Muñoa, M. Mouriño, Y. Jubete, F. De la Cruz, and A. Juárez. 1993. Escherichia coli hha mutants, DNA supercoiling and expression of haemolysin genes from recombinant plasmid pANN202-312. Mol. Microbiol. 9:1011-1018.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1011-1018
    • Carmona, M.1    Balsalobre, C.2    Muñoa, F.J.3    Mouriño, M.4    Jubete, Y.5    De La Cruz, F.6    Juárez, A.7
  • 5
    • 0033970889 scopus 로고    scopus 로고
    • Multimeric self-assembly equilibria involving the histone-like protein H-NS, a thermodynamic study
    • Ceschini, S., G. Lupidi, M. Coletta, C. L. Pon, E. Fioretti, and M. Angeletti. 2000. Multimeric self-assembly equilibria involving the histone-like protein H-NS, a thermodynamic study. J. Biol. Chem. 275:729-734.
    • (2000) J. Biol. Chem. , vol.275 , pp. 729-734
    • Ceschini, S.1    Lupidi, G.2    Coletta, M.3    Pon, C.L.4    Fioretti, E.5    Angeletti, M.6
  • 7
    • 0027407858 scopus 로고
    • Lentivirus envelope sequences and proviral genomes are stabilized in Escherichia coli when cloned in low-copy-number plasmid vectors
    • Cunningham, T. P., R. C. Montelaro, and K. E. Rushlow. 1993. Lentivirus envelope sequences and proviral genomes are stabilized in Escherichia coli when cloned in low-copy-number plasmid vectors. Gene 9:93-98.
    • (1993) Gene , vol.9 , pp. 93-98
    • Cunningham, T.P.1    Montelaro, R.C.2    Rushlow, K.E.3
  • 8
    • 2442560235 scopus 로고    scopus 로고
    • H-NS: A universal regulator for a dynamic genome
    • Dorman, C. J. 2004. H-NS: a universal regulator for a dynamic genome. Nat. Rev. Microbiol. 2:391-400.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 391-400
    • Dorman, C.J.1
  • 10
    • 0034751820 scopus 로고    scopus 로고
    • Hha is a negative modulator of transcription of hiLA, the Salmonella enterica serovar Typhimurium invasion gene transcriptional activator
    • Fahlen, T. F., R. L. Wilson, J. D. Boddicker, and B. D. Jones. 2001. Hha is a negative modulator of transcription of hiLA, the Salmonella enterica serovar Typhimurium invasion gene transcriptional activator. J. Bacteriol. 183:6620-6629.
    • (2001) J. Bacteriol. , vol.183 , pp. 6620-6629
    • Fahlen, T.F.1    Wilson, R.L.2    Boddicker, J.D.3    Jones, B.D.4
  • 11
    • 0035167187 scopus 로고    scopus 로고
    • Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein
    • Free, A., M. E. Porter, P. Deighan, and C. J. Dorman. 2001. Requirement for the molecular adapter function of StpA at the Escherichia coli bgl promoter depends upon the level of truncated H-NS protein. Mol. Microbiol. 42:903-917.
    • (2001) Mol. Microbiol. , vol.42 , pp. 903-917
    • Free, A.1    Porter, M.E.2    Deighan, P.3    Dorman, C.J.4
  • 12
    • 0026055806 scopus 로고
    • Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies
    • Hoffman, A., and R. G. Roeder. 1991. Purification of His-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies. Nucleic Acids Res. 19:6337-6338.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6337-6338
    • Hoffman, A.1    Roeder, R.G.2
  • 14
    • 0031757173 scopus 로고    scopus 로고
    • H-NS and StpA proteins stimulate expression of the maltose regulon in Escherichia coli
    • Johansson, J., B. Dagberg, E. Richet, and B. E. Uhlin. 1998. H-NS and StpA proteins stimulate expression of the maltose regulon in Escherichia coli. J. Bacteriol. 180:6117-6125.
    • (1998) J. Bacteriol. , vol.180 , pp. 6117-6125
    • Johansson, J.1    Dagberg, B.2    Richet, E.3    Uhlin, B.E.4
  • 15
    • 0035078382 scopus 로고    scopus 로고
    • Heteromeric interactions among nucleoid-associated bacterial proteins: Localization of StpA-stabilizing regions in H-NS of Escherichia coli
    • Johansson, J., S. Eriksson, B. Sondén, S. N. Wai, and B. E. Uhlin. 2001. Heteromeric interactions among nucleoid-associated bacterial proteins: localization of StpA-stabilizing regions in H-NS of Escherichia coli. J. Bacteriol. 183:2343-2347.
    • (2001) J. Bacteriol. , vol.183 , pp. 2343-2347
    • Johansson, J.1    Eriksson, S.2    Sondén, B.3    Wai, S.N.4    Uhlin, B.E.5
  • 16
    • 0032825041 scopus 로고    scopus 로고
    • Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli
    • Johansson, J., and B. E. Uhlin. 1999. Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli. Proc. Natl. Acad. Sci. USA 96:10776-10781.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10776-10781
    • Johansson, J.1    Uhlin, B.E.2
  • 17
    • 0021732545 scopus 로고
    • Expression and regulation of the plasmid-encoded haemolysin determinant of Escherichia coli
    • Juárez, A., C. Hughes, M. Vogel, and W. Goebel. 1984. Expression and regulation of the plasmid-encoded haemolysin determinant of Escherichia coli. Mol. Gen. Genet. 197:196-203.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 196-203
    • Juárez, A.1    Hughes, C.2    Vogel, M.3    Goebel, W.4
  • 18
    • 0024314489 scopus 로고
    • A locus involved in kanamycin, chloramphenicol and L-serine resistance is located in the bglY-galU region of the Escherichia coli K12 chromosome
    • Lejeune, P., P. Bertin, C. Walon, K. Willemot, C. Colson, and A. Danchin. 1989. A locus involved in kanamycin, chloramphenicol and L-serine resistance is located in the bglY-galU region of the Escherichia coli K12 chromosome. Mol. Gen. Genet. 218:361-363.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 361-363
    • Lejeune, P.1    Bertin, P.2    Walon, C.3    Willemot, K.4    Colson, C.5    Danchin, A.6
  • 19
    • 0036197713 scopus 로고    scopus 로고
    • Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors
    • Madrid, C., J. M. Nieto, and A. Juárez. 2002. Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors. Int. J. Med. Microbiol. 291:425-432.
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 425-432
    • Madrid, C.1    Nieto, J.M.2    Juárez, A.3
  • 20
    • 0036723747 scopus 로고    scopus 로고
    • Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin
    • Madrid, C., J. M. Nieto, S. Paytubí, F. Falconi, C. O. Gualerzi, C. O., and A. Juárez. 2002. Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin. J. Bacteriol. 184:5058-5066.
    • (2002) J. Bacteriol. , vol.184 , pp. 5058-5066
    • Madrid, C.1    Nieto, J.M.2    Paytubí, S.3    Falconi, F.4    Gualerzi, C.O.5    O, C.6    Juárez, A.7
  • 21
    • 0028225725 scopus 로고
    • A new class of proteins regulating gene expression in enterobacteria
    • Mikulskis, A. V., and G. Cornells. 1994. A new class of proteins regulating gene expression in enterobacteria. Mol. Microbiol. 11:77-86.
    • (1994) Mol. Microbiol. , vol.11 , pp. 77-86
    • Mikulskis, A.V.1    Cornells, G.2
  • 26
    • 0036174055 scopus 로고    scopus 로고
    • Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins
    • Nieto, J. M., C. Madrid, E. Miquelay, J. L. Parra, S. Rodríguez, and A. Juárez. 2002. Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins. J. Bacteriol. 184:629-635.
    • (2002) J. Bacteriol. , vol.184 , pp. 629-635
    • Nieto, J.M.1    Madrid, C.2    Miquelay, E.3    Parra, J.L.4    Rodríguez, S.5    Juárez, A.6
  • 27
    • 0033797058 scopus 로고    scopus 로고
    • Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS
    • Nieto, J. M., C. Madrid, A. Prenafeta, E. Miquelay, C. Balsalobre, M. Carrascal, and A. Juárez. 2000. Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS. Mol. Gen. Genet. 263:349-358.
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 349-358
    • Nieto, J.M.1    Madrid, C.2    Prenafeta, A.3    Miquelay, E.4    Balsalobre, C.5    Carrascal, M.6    Juárez, A.7
  • 28
    • 0019508392 scopus 로고
    • Determination of the functions of hemolytic plasmid pHly152 of Escherichia coli
    • Noegel, A., U. Rdest, and W. Goebel. 1981. Determination of the functions of hemolytic plasmid pHly152 of Escherichia coli. J. Bacteriol. 145:233-247.
    • (1981) J. Bacteriol. , vol.145 , pp. 233-247
    • Noegel, A.1    Rdest, U.2    Goebel, W.3
  • 30
    • 1842453825 scopus 로고    scopus 로고
    • Structure of the histone-like protein H-NS and its role in regulation and genome superstructure
    • Rimsky, S. 2004. Structure of the histone-like protein H-NS and its role in regulation and genome superstructure. Curr. Opin. Microbiol. 7:109-114.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 109-114
    • Rimsky, S.1
  • 31
    • 0023472472 scopus 로고
    • Tricine-Sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-Sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 32
    • 0041322572 scopus 로고    scopus 로고
    • The small nucleoid-binding proteins H-NS, HU, and Fis affect hilA expression in Salmonella enterica serovar Typhimurium
    • Schechter, L. M., S. Jain, S. Akbar, and C. A. Lee. 2003. The small nucleoid-binding proteins H-NS, HU, and Fis affect hilA expression in Salmonella enterica serovar Typhimurium. Infect. Immun. 71:5432-5435.
    • (2003) Infect. Immun. , vol.71 , pp. 5432-5435
    • Schechter, L.M.1    Jain, S.2    Akbar, S.3    Lee, C.A.4
  • 33
    • 0036332716 scopus 로고    scopus 로고
    • The bacterial regulatory protein H-NS. A versatile modulator of nucleic acid structures
    • Schröder, O., and R. Wagner. 2002. The bacterial regulatory protein H-NS. A versatile modulator of nucleic acid structures. Biol. Chem. 383:945-960.
    • (2002) Biol. Chem. , vol.383 , pp. 945-960
    • Schröder, O.1    Wagner, R.2
  • 34
    • 6044274611 scopus 로고    scopus 로고
    • Role of hha and ler in transcriptional regulation of the esp operon of enterohemorrhagic Escherichia coli O157:H7
    • Sharma, V. K., and R. L. Zuerner. 2004. Role of hha and ler in transcriptional regulation of the esp operon of enterohemorrhagic Escherichia coli O157:H7. J. Bacteriol. 186:7290-7301.
    • (2004) J. Bacteriol. , vol.186 , pp. 7290-7301
    • Sharma, V.K.1    Zuerner, R.L.2
  • 35
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber, V., C. A. Martinez, and F. H. Arnold. 2001. Libraries of hybrid proteins from distantly related sequences. Nat. Biotechnol. 19:456-460.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 38
    • 0242289416 scopus 로고    scopus 로고
    • H-NS in gram-negative bacteria: A family of multifaceted proteins
    • Tendeng, C., and P. Bertin. 2003. H-NS in gram-negative bacteria: a family of multifaceted proteins. Trends Microbiol. 11:511-518.
    • (2003) Trends Microbiol. , vol.11 , pp. 511-518
    • Tendeng, C.1    Bertin, P.2
  • 39
    • 0029785418 scopus 로고    scopus 로고
    • Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using dominant negative derivatives
    • Williams, R. M., S. Rimsky, and H. Buc. 1996. Probing the structure, function, and interactions of the Escherichia coli H-NS and StpA proteins by using dominant negative derivatives. J. Bacteriol. 178:4335-4343.
    • (1996) J. Bacteriol. , vol.178 , pp. 4335-4343
    • Williams, R.M.1    Rimsky, S.2    Buc, H.3
  • 40
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequencing of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and M. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequencing of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, M.3
  • 42
    • 0029913710 scopus 로고    scopus 로고
    • Escherichia coli protein analogs StpA and H-NS: Regulatory loops, similar and disparate effects on nucleic acid dynamics
    • Zhang, A., S. Rimsky, M. E. Reaban, H. Buc, and M. Belfort. 1996. Escherichia coli protein analogs StpA and H-NS: regulatory loops, similar and disparate effects on nucleic acid dynamics. EMBO J. 15:1340-1349.
    • (1996) EMBO J. , vol.15 , pp. 1340-1349
    • Zhang, A.1    Rimsky, S.2    Reaban, M.E.3    Buc, H.4    Belfort, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.