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Volumn 5, Issue 9, 2010, Pages 1-10

DNA clasping by mycobacterial HU: The c-terminal region of HupB mediates increased specificity of DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DEOXYRIBONUCLEASE I; HU PROTEIN; PLASMID DNA; PROTEIN HUPB; UNCLASSIFIED DRUG; BACTERIAL DNA; DNA BINDING PROTEIN; HISTONE; HISTONE LIKE PROTEIN HU, BACTERIA; HISTONE-LIKE PROTEIN HU, BACTERIA; HUPB PROTEIN, MYCOBACTERIUM TUBERCULOSIS;

EID: 77958585144     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012551     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0343794843 scopus 로고
    • Characterization of a novel, low-molecular weight DNA-binding protein from Escherichia coli
    • Rouviere-Yaniv J, Gros F (1975) Characterization of a novel, low-molecular weight DNA-binding protein from Escherichia coli Proc Natl Acad Sci USA 72: 3428-3432.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3428-3432
    • Rouviere-Yaniv, J.1    Gros, F.2
  • 2
    • 0018405881 scopus 로고
    • E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA
    • Rouviere-Yaniv J, Yaniv M, Germond JE (1979) E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA. Cell 17: 265-274.
    • (1979) Cell , vol.17 , pp. 265-274
    • Rouviere-Yaniv, J.1    Yaniv, M.2    Germond, J.E.3
  • 3
    • 0031576352 scopus 로고    scopus 로고
    • Variation in HU composition during growth of Escherichia coli: The heterodimer is required for long term survival
    • Claret L, Rouviere-Yaniv J (1997) Variation in HU composition during growth of Escherichia coli: the heterodimer is required for long term survival. J Mol Biol 273: 93-104.
    • (1997) J Mol Biol , vol.273 , pp. 93-104
    • Claret, L.1    Rouviere-Yaniv, J.2
  • 4
    • 0018803622 scopus 로고
    • Amino and carboxy terminal sequences of the DNA-binding protein HU from the Cyanobacterium Synechocystis PCC 6701 (ATCC 27170)
    • Aitken A, Rouviere-Yaniv J (1979) Amino and carboxy terminal sequences of the DNA-binding protein HU from the Cyanobacterium Synechocystis PCC 6701 (ATCC 27170). Biochem Biophys Res Commun 91: 461-467.
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 461-467
    • Aitken, A.1    Rouviere-Yaniv, J.2
  • 5
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam TA, Ishihama A (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J Biol Chem 274: 33105-33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 6
    • 0035077003 scopus 로고    scopus 로고
    • HU-GFP and DAPI co-localize on the Escherichia coli nucleoid
    • Wery M, Woldringh C, Rouviere-Yaniv J (2001) HU-GFP and DAPI co-localize on the Escherichia coli nucleoid. Biochimie (Paris) 83: 193-200.
    • (2001) Biochimie (Paris) , vol.83 , pp. 193-200
    • Wery, M.1    Woldringh, C.2    Rouviere-Yaniv, J.3
  • 7
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam TA, Hiraga S, Ishihama A (2000) Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes Cells 5: 613-626.
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.A.1    Hiraga, S.2    Ishihama, A.3
  • 8
    • 0023413620 scopus 로고
    • Histonelike proteins of bacteria
    • Drlica K, Rouviere-Yaniv J (1987) Histonelike proteins of bacteria. Microbiol Rev 51: 301-319.
    • (1987) Microbiol Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 10
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA
    • Pinson V, Takahashi M, Rouviere-Yaniv J (1999) Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA. J Mol Biol 287: 485-497.
    • (1999) J Mol Biol , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 11
    • 0029061514 scopus 로고
    • Increased sensitivity to gamma irradiation in bacteria lacking protein HU
    • Boubrik F, Rouviere-Yaniv J (1995) Increased sensitivity to gamma irradiation in bacteria lacking protein HU. Proc Natl Acad Sci U S A 92: 3958-3962.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3958-3962
    • Boubrik, F.1    Rouviere-Yaniv, J.2
  • 12
    • 0031858092 scopus 로고    scopus 로고
    • Escherichia coli Strains Lacking Protein HU Are UV Sensitive due to a Role for HU in Homologous Recombination
    • Li S, Waters R (1998) Escherichia coli Strains Lacking Protein HU Are UV Sensitive due to a Role for HU in Homologous Recombination. J Bacteriol 180: 3750-3756.
    • (1998) J Bacteriol , vol.180 , pp. 3750-3756
    • Li, S.1    Waters, R.2
  • 13
    • 0023766613 scopus 로고
    • A model for initiation at origins of DNA replication
    • Bramhill D, Kornberg A (1988) A model for initiation at origins of DNA replication. Cell 54: 915-918.
    • (1988) Cell , vol.54 , pp. 915-918
    • Bramhill, D.1    Kornberg, A.2
  • 14
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang DS, Kornberg A (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J Biol Chem 267: 23083-23086.
    • (1992) J Biol Chem , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 15
    • 0029973105 scopus 로고    scopus 로고
    • Anatomy of a flexer-DNA complex inside a higher-order transposition intermediate
    • Lavoie BD, Shaw GS, Millner A, Chaconas G (1996) Anatomy of a flexer-DNA complex inside a higher-order transposition intermediate. Cell 85: 761-771.
    • (1996) Cell , vol.85 , pp. 761-771
    • Lavoie, B.D.1    Shaw, G.S.2    Millner, A.3    Chaconas, G.4
  • 17
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger KK, Lemberg KM, Zhang Y, Rice PA (2003) Flexible DNA bending in HU-DNA cocrystal structures. Embo J 22: 3749-3760.
    • (2003) Embo J , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 18
    • 0023644961 scopus 로고
    • The integration host factor of Escherichia coli binds to bent DNA at the origin of replication of the plasmid pSC101
    • Stenzel TT, Patel P, Bastia D (1987) The integration host factor of Escherichia coli binds to bent DNA at the origin of replication of the plasmid pSC101. Cell 49: 709-717.
    • (1987) Cell , vol.49 , pp. 709-717
    • Stenzel, T.T.1    Patel, P.2    Bastia, D.3
  • 19
    • 49749148015 scopus 로고    scopus 로고
    • The C-terminal domain of HU-related histone-like protein Hlp from Mycobacterium smegmatis mediates DNA end-joining
    • Mukherjee A, Bhattacharyya G, Grove A (2008) The C-terminal domain of HU-related histone-like protein Hlp from Mycobacterium smegmatis mediates DNA end-joining. Biochemistry 47: 8744-8753.
    • (2008) Biochemistry , vol.47 , pp. 8744-8753
    • Mukherjee, A.1    Bhattacharyya, G.2    Grove, A.3
  • 20
    • 0026019440 scopus 로고
    • HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments
    • Bonnefoy E, Rouvière-Yaniv J (1991) HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments. EMBO J 10: 687-696.
    • (1991) EMBO J , vol.10 , pp. 687-696
    • Bonnefoy, E.1    Rouvière-Yaniv, J.2
  • 21
    • 0033214062 scopus 로고    scopus 로고
    • The binding motif recognized by HU on both nicked and cruciform DNA
    • Kamashev D, Balandina A, Rouviere-Yaniv J (1999) The binding motif recognized by HU on both nicked and cruciform DNA. EMBO J 18: 5434-5444.
    • (1999) EMBO J , vol.18 , pp. 5434-5444
    • Kamashev, D.1    Balandina, A.2    Rouviere-Yaniv, J.3
  • 22
    • 0022545522 scopus 로고
    • Host protein requirements for in vitro site-specific DNA inversion
    • Johnson RC, Bruist MF, Simon MI (1986) Host protein requirements for in vitro site-specific DNA inversion. Cell 46: 531-539.
    • (1986) Cell , vol.46 , pp. 531-539
    • Johnson, R.C.1    Bruist, M.F.2    Simon, M.I.3
  • 23
    • 0025897381 scopus 로고
    • Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu
    • Micka B, Groch N, Heinemann U, Marahiel MA (1991) Molecular cloning, nucleotide sequence, and characterization of the Bacillus subtilis gene encoding the DNA-binding protein HBsu. J Bacteriol 173: 3191-3198.
    • (1991) J Bacteriol , vol.173 , pp. 3191-3198
    • Micka, B.1    Groch, N.2    Heinemann, U.3    Marahiel, M.A.4
  • 24
    • 0034022882 scopus 로고    scopus 로고
    • The Bacillus subtilis HBsu protein modifies the effects of alpha/beta-type, small acid-soluble spore proteins on DNA
    • Ross MA, Setlow P (2000) The Bacillus subtilis HBsu protein modifies the effects of alpha/beta-type, small acid-soluble spore proteins on DNA. J Bacteriol 182: 1942-1948.
    • (2000) J Bacteriol , vol.182 , pp. 1942-1948
    • Ross, M.A.1    Setlow, P.2
  • 25
    • 0032457805 scopus 로고    scopus 로고
    • Identification of an immunogenic histone-like protein (HLPMt) of Mycobacte-rium tuberculosis
    • Prabhakar S, Annapurna PS, Jain NK, Dey AB, Tyagi JS, et al. (1998) Identification of an immunogenic histone-like protein (HLPMt) of Mycobacte-rium tuberculosis. Tuber Lung Dis 79: 43-53.
    • (1998) Tuber Lung Dis , vol.79 , pp. 43-53
    • Prabhakar, S.1    Annapurna, P.S.2    Jain, N.K.3    Dey, A.B.4    Tyagi, J.S.5
  • 26
    • 0034974503 scopus 로고    scopus 로고
    • Identification of the mycobacterial DNA-binding protein 1 region which suppresses transcription in vitro
    • Furugen M, Matsumoto S, Matsuo T, Matsumoto M, Yamada T (2001) Identification of the mycobacterial DNA-binding protein 1 region which suppresses transcription in vitro. Microb Pathog 30: 129-138.
    • (2001) Microb Pathog , vol.30 , pp. 129-138
    • Furugen, M.1    Matsumoto, S.2    Matsuo, T.3    Matsumoto, M.4    Yamada, T.5
  • 27
    • 2942620506 scopus 로고    scopus 로고
    • Use of the hupB gene encoding a histone-like protein of Mycobacterium tuberculosis as a target for detection and differentiation of M. tuberculosis and M
    • Prabhakar S, Mishra A, Singhal A, Katoch VM, Thakral SS, et al. (2004) Use of the hupB gene encoding a histone-like protein of Mycobacterium tuberculosis as a target for detection and differentiation of M. tuberculosis and M. bovis. J Clin Microbiol 42: 2724-2732.
    • (2004) Bovis. J Clin Microbiol , vol.42 , pp. 2724-2732
    • Prabhakar, S.1    Mishra, A.2    Singhal, A.3    Katoch, V.M.4    Thakral, S.S.5
  • 28
    • 0036892211 scopus 로고    scopus 로고
    • Decreased infectivity despite unaltered C3 binding by a Delta hbhA mutant of Mycobacterium tuberculosis
    • Mueller-Ortiz SL, Sepulveda E, Olsen MR, Jagannath C, Wanger AR, et al. (2002) Decreased infectivity despite unaltered C3 binding by a Delta hbhA mutant of Mycobacterium tuberculosis. Infect Immun 70: 6751-6760.
    • (2002) Infect Immun , vol.70 , pp. 6751-6760
    • Mueller-Ortiz, S.L.1    Sepulveda, E.2    Olsen, M.R.3    Jagannath, C.4    Wanger, A.R.5
  • 29
    • 0021753304 scopus 로고
    • Proteins from the prokaryotic nucleiod. High-resolution 1H NMR spectroscopic study of Escherichia coli DNA-binding proteins NS1 and NS2
    • Paci M, Pon CL, Losso MA, Gualerzi CO (1984) Proteins from the prokaryotic nucleiod. High-resolution 1H NMR spectroscopic study of Escherichia coli DNA-binding proteins NS1 and NS2. Eur J Biochem 138: 193-200.
    • (1984) Eur J Biochem , vol.138 , pp. 193-200
    • Paci, M.1    Pon, C.L.2    Losso, M.A.3    Gualerzi, C.O.4
  • 30
    • 0034416406 scopus 로고    scopus 로고
    • The histone-like protein HU binds specifically to DNA recombination and repair intermediates
    • Kamashev D, Rouviere-Yaniv J (2000) The histone-like protein HU binds specifically to DNA recombination and repair intermediates. EMBO J 19: 6527-6535.
    • (2000) EMBO J , vol.19 , pp. 6527-6535
    • Kamashev, D.1    Rouviere-Yaniv, J.2
  • 31
    • 0026532533 scopus 로고
    • Preferential binding of E.coli histone-like protein HU alpha to negatively supercoiled DNA
    • Shindo H, Furubayashi A, Shimizu M, Miyake M, Imamoto F (1992) Preferential binding of E.coli histone-like protein HU alpha to negatively supercoiled DNA. Nucleic Acids Res 20: 1553-1558.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1553-1558
    • Shindo, H.1    Furubayashi, A.2    Shimizu, M.3    Miyake, M.4    Imamoto, F.5
  • 32
    • 33846025466 scopus 로고    scopus 로고
    • Right-handed DNA supercoiling by an octameric form of histone-like protein HU: Modulation of cellular transcription
    • Kar S, Choi EJ, Guo F, Dimitriadis EK, Kotova SL, et al. (2006) Right-handed DNA supercoiling by an octameric form of histone-like protein HU: modulation of cellular transcription. J Biol Chem 281: 40144-40153.
    • (2006) J Biol Chem , vol.281 , pp. 40144-40153
    • Kar, S.1    Choi, E.J.2    Guo, F.3    Dimitriadis, E.K.4    Kotova, S.L.5
  • 33
    • 0017021328 scopus 로고
    • Prokaryotic DNA in nucleoid structure
    • Pettijohn DE (1976) Prokaryotic DNA in nucleoid structure. CRC Crit Rev Biochem 4: 175-202.
    • (1976) CRC Crit Rev Biochem , vol.4 , pp. 175-202
    • Pettijohn, D.E.1
  • 34
    • 18444369954 scopus 로고    scopus 로고
    • The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin
    • Dame RT (2005) The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Mol Microbiol 56: 858-870.
    • (2005) Mol Microbiol , vol.56 , pp. 858-870
    • Dame, R.T.1
  • 35
    • 33845796196 scopus 로고    scopus 로고
    • Structure-based analysis of HU-DNA binding
    • Swinger KK, Rice PA (2007) Structure-based analysis of HU-DNA binding. J Mol Biol 365: 1005-1016.
    • (2007) J Mol Biol , vol.365 , pp. 1005-1016
    • Swinger, K.K.1    Rice, P.A.2
  • 36
    • 58349095446 scopus 로고    scopus 로고
    • In-vitro helix opening of M. tuberculosis oriC by DnaA occurs at precise location and is inhibited by IciA like protein
    • Kumar S, Farhana A, Hasnain SE (2009) In-vitro helix opening of M. tuberculosis oriC by DnaA occurs at precise location and is inhibited by IciA like protein. PLoS ONE 4: e4139.
    • (2009) PLoS ONE , vol.4
    • Kumar, S.1    Farhana, A.2    Hasnain, S.E.3
  • 37
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH, Rubin EJ (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48: 77-84.
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 39
    • 21244483507 scopus 로고    scopus 로고
    • Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity
    • Prakash P, Aruna B, Sardesai AA, Hasnain SE (2005) Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity. J Biol Chem 280: 19641-19648.
    • (2005) J Biol Chem , vol.280 , pp. 19641-19648
    • Prakash, P.1    Aruna, B.2    Sardesai, A.A.3    Hasnain, S.E.4


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