메뉴 건너뛰기




Volumn 291, Issue 2, 2009, Pages 232-240

Mycobacterium smegmatis histone-like protein Hlp is nucleoid associated: Research Letter

Author keywords

DAPI staining; DNA binding protein; Hlp; HU; Immunofluorescence microscopy; In vivo localization

Indexed keywords

GENOMIC DNA; HISTONE; LAMININ;

EID: 58449100290     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2008.01458.x     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0037129959 scopus 로고    scopus 로고
    • Identification of 34 amino acid stretch within the C-terminus of histone H1 as the DNA-condensing domain by site directed mutagenesis
    • Bharath MM, Ramesh S, Chandra NR Rao MR (2002) Identification of 34 amino acid stretch within the C-terminus of histone H1 as the DNA-condensing domain by site directed mutagenesis. Biochemistry 41 : 7617 7627.
    • (2002) Biochemistry , vol.41 , pp. 7617-7627
    • Bharath, M.M.1    Ramesh, S.2    Chandra, N.R.3    Rao, M.R.4
  • 3
    • 33646396203 scopus 로고    scopus 로고
    • Permeabilization of the mycobacterial envelope for protein cytolocalization studies by immunofluorescence microscopy
    • Cimino M, Alamo L Salazar L (2006) Permeabilization of the mycobacterial envelope for protein cytolocalization studies by immunofluorescence microscopy. BMC Microbiol 6 : 35 39.
    • (2006) BMC Microbiol , vol.6 , pp. 35-39
    • Cimino, M.1    Alamo, L.2    Salazar, L.3
  • 4
    • 0023711642 scopus 로고
    • Alpha-helix in the carboxy-terminal domains of histones H1 and H5
    • Clark DJ, Hill CS, Martin SR Thomas JO (1988) Alpha-helix in the carboxy-terminal domains of histones H1 and H5. EMBO J 7 : 69 75.
    • (1988) EMBO J , vol.7 , pp. 69-75
    • Clark, D.J.1    Hill, C.S.2    Martin, S.R.3    Thomas, J.O.4
  • 5
    • 0032750280 scopus 로고    scopus 로고
    • Identification of a novel mycobacterial histone H1 homologue (HupB) as an antigenic target of pANCA monoclonal antibody and serum immunoglobulin A from patients with Crohn's disease
    • Cohavy O, Harth G, Horwitz M, Eggena M, Landers C, Sutton C, Targan SR Braun J (1999) Identification of a novel mycobacterial histone H1 homologue (HupB) as an antigenic target of pANCA monoclonal antibody and serum immunoglobulin A from patients with Crohn's disease. Infect Immun 67 : 6510 6517.
    • (1999) Infect Immun , vol.67 , pp. 6510-6517
    • Cohavy, O.1    Harth, G.2    Horwitz, M.3    Eggena, M.4    Landers, C.5    Sutton, C.6    Targan, S.R.7    Braun, J.8
  • 6
    • 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
  • 7
    • 32244443761 scopus 로고    scopus 로고
    • The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin binding protein for cell division
    • Dasgupta A, Datta P, Kundu M Basu J (2006) The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin binding protein for cell division. Microbiology 152 : 493 504.
    • (2006) Microbiology , vol.152 , pp. 493-504
    • Dasgupta, A.1    Datta, P.2    Kundu, M.3    Basu, J.4
  • 8
    • 0032526681 scopus 로고    scopus 로고
    • Oxygen depletion induced dormancy in Mycobacterium smegmatis
    • Dick T, Lee BH Murugasu-Oei B (1998) Oxygen depletion induced dormancy in Mycobacterium smegmatis. FEMS Microbiol Lett 163 : 159 164.
    • (1998) FEMS Microbiol Lett , vol.163 , pp. 159-164
    • Dick, T.1    Lee, B.H.2    Murugasu-Oei, B.3
  • 9
    • 0025371343 scopus 로고
    • Nucleolin from the multiple nucleoli of amphibian oocyte nuclei
    • DiMario PJ Gall JG (1990) Nucleolin from the multiple nucleoli of amphibian oocyte nuclei. Chromosoma 99 : 87 94.
    • (1990) Chromosoma , vol.99 , pp. 87-94
    • Dimario, P.J.1    Gall, J.G.2
  • 11
    • 2942748432 scopus 로고    scopus 로고
    • Linker histone interaction shows divalent character with both supercoiled and linear DNA
    • Ellen TP van Holde KE (2004) Linker histone interaction shows divalent character with both supercoiled and linear DNA. Biochemistry 43 : 7867 7872.
    • (2004) Biochemistry , vol.43 , pp. 7867-7872
    • Ellen, T.P.1    Van Holde, K.E.2
  • 12
    • 32344450783 scopus 로고    scopus 로고
    • The Deinococcus radiodurans-encoded HU protein has two DNA-binding domains
    • Ghosh S Grove A (2006) The Deinococcus radiodurans-encoded HU protein has two DNA-binding domains. Biochemistry 45 : 1723 1733.
    • (2006) Biochemistry , vol.45 , pp. 1723-1733
    • Ghosh, S.1    Grove, A.2
  • 13
    • 0035902820 scopus 로고    scopus 로고
    • High-affinity DNA binding of HU protein from the hyperthermophile Thermotoga maritima
    • Grove A Lim L (2001) High-affinity DNA binding of HU protein from the hyperthermophile Thermotoga maritima. J Mol Biol 311 : 491 502.
    • (2001) J Mol Biol , vol.311 , pp. 491-502
    • Grove, A.1    Lim, L.2
  • 14
    • 0032190355 scopus 로고    scopus 로고
    • Increased alanine dehydrogenase activity during dormancy in Mycobacterium smegmatis
    • Hutter B Dick T (1998) Increased alanine dehydrogenase activity during dormancy in Mycobacterium smegmatis. FEMS Microbiol Lett 167 : 7 11.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 7-11
    • Hutter, B.1    Dick, T.2
  • 15
    • 0026920680 scopus 로고
    • Autoantibodies to nucleolin cross-react with histone H1 in systemic lupus erythematosus
    • Jarjour WN, Minota S, Roubey RA, Mimura T Winfield JB (1992) Autoantibodies to nucleolin cross-react with histone H1 in systemic lupus erythematosus. Mol Biol Rep 16 : 263 266.
    • (1992) Mol Biol Rep , vol.16 , pp. 263-266
    • Jarjour, W.N.1    Minota, S.2    Roubey, R.A.3    Mimura, T.4    Winfield, J.B.5
  • 16
    • 0026685334 scopus 로고
    • Chromatins of low-protein-content: Special features of their compaction and condensation
    • Kellenberger E Arnold-Schultz-Gahmen B (1992) Chromatins of low-protein-content: special features of their compaction and condensation. FEMS Microbiol Lett 100 : 361 370.
    • (1992) FEMS Microbiol Lett , vol.100 , pp. 361-370
    • Kellenberger, E.1    Arnold-Schultz-Gahmen, B.2
  • 18
    • 0030904358 scopus 로고    scopus 로고
    • Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis
    • Köhler P Marahiel MA (1997) Association of the histone-like protein HBsu with the nucleoid of Bacillus subtilis. J Bacteriol 179 : 2060 2064.
    • (1997) J Bacteriol , vol.179 , pp. 2060-2064
    • Köhler, P.1    Marahiel, M.A.2
  • 20
    • 0032432632 scopus 로고    scopus 로고
    • Upregulation of a histone-like protein in dormant Mycobacterium smegmatis
    • Lee BH, Murugasu-Oei B Dick T (1998) Upregulation of a histone-like protein in dormant Mycobacterium smegmatis. Mol Gen Genet 260 : 475 479.
    • (1998) Mol Gen Genet , vol.260 , pp. 475-479
    • Lee, B.H.1    Murugasu-Oei, B.2    Dick, T.3
  • 22
    • 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 (2008a) 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
  • 23
    • 47249161238 scopus 로고    scopus 로고
    • DNA compaction by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima
    • Mukherjee A, Sokunbi AO Grove A (2008b) DNA compaction by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima. Nucleic Acids Res 36 : 3956 3968.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3956-3968
    • Mukherjee, A.1    Sokunbi, A.O.2    Grove, A.3
  • 24
    • 15944387317 scopus 로고    scopus 로고
    • The viable but nonculturable state in bacteria
    • Oliver JD (2005) The viable but nonculturable state in bacteria. J Microbiol 43 : 93 100.
    • (2005) J Microbiol , vol.43 , pp. 93-100
    • Oliver, J.D.1
  • 25
    • 0035849873 scopus 로고    scopus 로고
    • The heparin binding haemagglutinin of Mycobacterium tuberculosis is required for extra pulmonary dissemination
    • Pethe K, Alonso S, Biet F, Delogu G, Brennan MJ, Locht C Menozzi FD (2001a) The heparin binding haemagglutinin of Mycobacterium tuberculosis is required for extra pulmonary dissemination. Nature 412 : 190 194.
    • (2001) Nature , vol.412 , pp. 190-194
    • Pethe, K.1    Alonso, S.2    Biet, F.3    Delogu, G.4    Brennan, M.J.5    Locht, C.6    Menozzi, F.D.7
  • 26
    • 0035181363 scopus 로고    scopus 로고
    • Mycobacterium smegmatis laminin-binding glycoprotein shares epitopes with Mycobacterium tuberculosis heparin-binding haemagglutinin
    • Pethe K, Puech V, Daffé M, Josenhans C, Drobecq H, Locht C Menozzi FD (2001b) Mycobacterium smegmatis laminin-binding glycoprotein shares epitopes with Mycobacterium tuberculosis heparin-binding haemagglutinin. Mol Microbiol 39 : 89 99.
    • (2001) Mol Microbiol , vol.39 , pp. 89-99
    • Pethe, K.1    Puech, V.2    Daffé, M.3    Josenhans, C.4    Drobecq, H.5    Locht, C.6    Menozzi, F.D.7
  • 28
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of IHF-DNA complex: A protein-induced U-turn
    • Rice PA, Yang S, Mizuuchi K Nash HA (1996) Crystal structure of IHF-DNA complex: a protein-induced U-turn. Cell 87 : 1295 1306.
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.2    Mizuuchi, K.3    Nash, H.A.4
  • 29
    • 0343794843 scopus 로고
    • Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli
    • Rouvière-Yaniv J Gros F (1975) Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli. P Natl Acad Sci USA 72 : 3428 3432.
    • (1975) P Natl Acad Sci USA , vol.72 , pp. 3428-3432
    • Rouvière-Yaniv, J.1    Gros, F.2
  • 30
    • 0035113470 scopus 로고    scopus 로고
    • The cold-shock stress response in Mycobacterium smegmatis includes the expression of a histone-like protein
    • Shires K Steyn L (2001) The cold-shock stress response in Mycobacterium smegmatis includes the expression of a histone-like protein. Mol Microbiol 39 : 994 1009.
    • (2001) Mol Microbiol , vol.39 , pp. 994-1009
    • Shires, K.1    Steyn, L.2
  • 32
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger KK, Lemberg KM, Zang 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    Zang, Y.3    Rice, P.A.4
  • 33
    • 0021286693 scopus 로고
    • 3-Å resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka I, Appelt K, Dijk J, White SW Wilson KS (1984) 3-Å resolution structure of a protein with histone-like properties in prokaryotes. Nature 310 : 376 381.
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 34
    • 0036050398 scopus 로고    scopus 로고
    • The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • Woldringh CL (2002) The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation. Mol Microbiol 45 : 17 29.
    • (2002) Mol Microbiol , vol.45 , pp. 17-29
    • Woldringh, C.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.