메뉴 건너뛰기




Volumn 319, Issue 2, 2011, Pages 106-114

Structure and function of a cold shock domain fold protein, CspD, in Janthinobacterium sp. Ant5-2 from East Antarctica

Author keywords

Betaproteobacteria; Cold adaptation; Cold shock protein; Psychrotolerant; UV radiation

Indexed keywords

COLD SHOCK PROTEIN; SINGLE STRANDED DNA;

EID: 79956128889     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02269.x     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0034608861 scopus 로고    scopus 로고
    • Escherichia coli CspA-family RNA chaperones are transcription antiterminators
    • Bae W, Xia B, Inouye M & Severinov K (2000) Escherichia coli CspA-family RNA chaperones are transcription antiterminators. P Natl Acad Sci USA 97: 7784-7789.
    • (2000) P Natl Acad Sci USA , vol.97 , pp. 7784-7789
    • Bae, W.1    Xia, B.2    Inouye, M.3    Severinov, K.4
  • 3
    • 3042615963 scopus 로고    scopus 로고
    • Systems level insights into the stress response to UV radiation in the halophilic archaeon Halobacterium NRC-1
    • Baliga NS, Bjork SJ, Bonneau R et al. (2004) Systems level insights into the stress response to UV radiation in the halophilic archaeon Halobacterium NRC-1. Genome Res 14: 1025-1035.
    • (2004) Genome Res , vol.14 , pp. 1025-1035
    • Baliga, N.S.1    Bjork, S.J.2    Bonneau, R.3
  • 4
    • 0033965637 scopus 로고    scopus 로고
    • Cold-tolerant alkane-degrading Rhodococcus species from Antarctica
    • Bej AK, Saul D & Aislabie J (2000) Cold-tolerant alkane-degrading Rhodococcus species from Antarctica. Polar Biol 23: 100-105.
    • (2000) Polar Biol , vol.23 , pp. 100-105
    • Bej, A.K.1    Saul, D.2    Aislabie, J.3
  • 5
    • 0034511264 scopus 로고    scopus 로고
    • Ribosomal DNA and resolution of branching order among the ascomycota: how many nucleotides are enough?
    • Berbee ML, Carmean DA & Winka K (2000) Ribosomal DNA and resolution of branching order among the ascomycota: how many nucleotides are enough? Mol Phylogenet Evol 17: 337-344.
    • (2000) Mol Phylogenet Evol , vol.17 , pp. 337-344
    • Berbee, M.L.1    Carmean, D.A.2    Winka, K.3
  • 6
    • 0030023653 scopus 로고    scopus 로고
    • Cold shock and cold acclimation proteins in the psychrotrophic bacterium Arthrobacter globiformis SI55
    • Berger F, Morellet N, Menu F & Potier P (1996) Cold shock and cold acclimation proteins in the psychrotrophic bacterium Arthrobacter globiformis SI55. J Bacteriol 178: 2999-3007.
    • (1996) J Bacteriol , vol.178 , pp. 2999-3007
    • Berger, F.1    Morellet, N.2    Menu, F.3    Potier, P.4
  • 9
    • 0032483047 scopus 로고    scopus 로고
    • Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site
    • Feng W, Tejero R, Zimmerman DE, Inouye M & Montelione GT (1998) Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site. Biochemistry 37: 10881-10896.
    • (1998) Biochemistry , vol.37 , pp. 10881-10896
    • Feng, W.1    Tejero, R.2    Zimmerman, D.E.3    Inouye, M.4    Montelione, G.T.5
  • 10
    • 0031463654 scopus 로고    scopus 로고
    • Detection and speciation of bacteria through PCR using universal major cold-shock protein primer oligomers
    • Francis KP & Stewart GS (1997) Detection and speciation of bacteria through PCR using universal major cold-shock protein primer oligomers. J Ind Microbiol Biot 19: 286-229.
    • (1997) J Ind Microbiol Biot , vol.19 , pp. 286-229
    • Francis, K.P.1    Stewart, G.S.2
  • 12
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann PL & Marahiel MA (1998) A superfamily of proteins that contain the cold-shock domain. Trends Biochem Sci 23: 286-290.
    • (1998) Trends Biochem Sci , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 13
    • 0029760156 scopus 로고    scopus 로고
    • Cold shock and cold acclimation protein in the psychrotrophic bacterium Pseudomonas putida Q5 and its transconjugants
    • Gumley WE & Inniss WE (1996) Cold shock and cold acclimation protein in the psychrotrophic bacterium Pseudomonas putida Q5 and its transconjugants. Can J Microbiol 42: 798-803.
    • (1996) Can J Microbiol , vol.42 , pp. 798-803
    • Gumley, W.E.1    Inniss, W.E.2
  • 14
    • 0031907673 scopus 로고    scopus 로고
    • Growth, survival and characterization of cspA in Salmonella enteritidis following cold shock
    • Jeffreys AG, Hak KM, Steffan RJ, Foster JW & Bej AK (1998) Growth, survival and characterization of cspA in Salmonella enteritidis following cold shock. Curr Microbiol 36: 29-35.
    • (1998) Curr Microbiol , vol.36 , pp. 29-35
    • Jeffreys, A.G.1    Hak, K.M.2    Steffan, R.J.3    Foster, J.W.4    Bej, A.K.5
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292: 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 16
    • 72949116993 scopus 로고    scopus 로고
    • Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli
    • Kim Y & Wood TK (2010) Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli. Biochem Bioph Res Co 391: 209-213.
    • (2010) Biochem Bioph Res Co , vol.391 , pp. 209-213
    • Kim, Y.1    Wood, T.K.2
  • 18
    • 0034844324 scopus 로고    scopus 로고
    • Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima
    • Kremer W, Schuler B, Harrieder S et al. (2001) Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima. Eur J Biochem 268: 2527-2539.
    • (2001) Eur J Biochem , vol.268 , pp. 2527-2539
    • Kremer, W.1    Schuler, B.2    Harrieder, S.3
  • 19
    • 33846991935 scopus 로고    scopus 로고
    • Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus
    • Max KE, Zeeb M, Bienert R, Balbach J & Heinemann U (2007) Common mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticus. FEBS J 274: 1265-1279.
    • (2007) FEBS J , vol.274 , pp. 1265-1279
    • Max, K.E.1    Zeeb, M.2    Bienert, R.3    Balbach, J.4    Heinemann, U.5
  • 20
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita RY (1975) Psychrophilic bacteria. Bacteriol Rev 39: 144-167.
    • (1975) Bacteriol Rev , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 21
    • 0034615784 scopus 로고    scopus 로고
    • Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein
    • Mueller U, Perl D, Schmid FX & Heinemann U (2000) Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein. J Mol Biol 297: 975-988.
    • (2000) J Mol Biol , vol.297 , pp. 975-988
    • Mueller, U.1    Perl, D.2    Schmid, F.X.3    Heinemann, U.4
  • 22
    • 0028234777 scopus 로고
    • Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA
    • Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M & Montelione GT (1994) Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA. P Natl Acad Sci USA 91: 5114-5118.
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 5114-5118
    • Newkirk, K.1    Feng, W.2    Jiang, W.3    Tejero, R.4    Emerson, S.D.5    Inouye, M.6    Montelione, G.T.7
  • 23
    • 67349137629 scopus 로고    scopus 로고
    • Identification of PprM: a modulator of the PprI-dependent DNA damage response in Deinococcus radiodurans
    • Ohba H, Satoh K, Sghaier H, Yanagisawa T & Narumi I (2009) Identification of PprM: a modulator of the PprI-dependent DNA damage response in Deinococcus radiodurans. Extremophiles 13: 471-479.
    • (2009) Extremophiles , vol.13 , pp. 471-479
    • Ohba, H.1    Satoh, K.2    Sghaier, H.3    Yanagisawa, T.4    Narumi, I.5
  • 24
    • 0036922947 scopus 로고    scopus 로고
    • Cold tolerance of Pseudomonas sp.30-3 isolated from oil-contaminated soil, Antarctica
    • Panicker G, Aislabie J, Saul D & Bej AK (2002) Cold tolerance of Pseudomonas sp.30-3 isolated from oil-contaminated soil, Antarctica. Polar Biol 25: 5-11.
    • (2002) Polar Biol , vol.25 , pp. 5-11
    • Panicker, G.1    Aislabie, J.2    Saul, D.3    Bej, A.K.4
  • 25
    • 77951767564 scopus 로고    scopus 로고
    • Occurrence and distribution of capB in Antarctic microorganisms and study of its structure and regulation in the Antarctic biodegradative Pseudomonas sp. 30/3
    • Panicker G, Mojib N, Nakatsuji T, Aislabie J & Bej AK (2010) Occurrence and distribution of capB in Antarctic microorganisms and study of its structure and regulation in the Antarctic biodegradative Pseudomonas sp. 30/3. Extremophiles 14: 171-183.
    • (2010) Extremophiles , vol.14 , pp. 171-183
    • Panicker, G.1    Mojib, N.2    Nakatsuji, T.3    Aislabie, J.4    Bej, A.K.5
  • 27
    • 1442277681 scopus 로고    scopus 로고
    • The mechanism of nucleic acid melting by a CspA family protein
    • Phadtare S, Inouye M & Severinov K (2004) The mechanism of nucleic acid melting by a CspA family protein. J Mol Biol 337: 147-155.
    • (2004) J Mol Biol , vol.337 , pp. 147-155
    • Phadtare, S.1    Inouye, M.2    Severinov, K.3
  • 28
    • 41949091189 scopus 로고    scopus 로고
    • Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer
    • Ren J, Nettleship JE, Sainsbury S, Saunders NJ & Owens RJ (2008) Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. Acta Crystallogr F 64: 247-251.
    • (2008) Acta Crystallogr F , vol.64 , pp. 247-251
    • Ren, J.1    Nettleship, J.E.2    Sainsbury, S.3    Saunders, N.J.4    Owens, R.J.5
  • 29
    • 77957242885 scopus 로고    scopus 로고
    • Ultra-fast FFT protein docking on graphics processors
    • Ritchie DW & Venkatraman V (2010) Ultra-fast FFT protein docking on graphics processors. Bioinformatics 26: 2398-2405.
    • (2010) Bioinformatics , vol.26 , pp. 2398-2405
    • Ritchie, D.W.1    Venkatraman, V.2
  • 30
    • 0028306109 scopus 로고
    • Crystal structure of CspA, the major cold shock protein of Escherichia coli
    • Schindelin H, Jiang W, Inouye M & Heinemann U (1994) Crystal structure of CspA, the major cold shock protein of Escherichia coli. P Natl Acad Sci USA 91: 5119-5123.
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 5119-5123
    • Schindelin, H.1    Jiang, W.2    Inouye, M.3    Heinemann, U.4
  • 31
    • 0033525071 scopus 로고    scopus 로고
    • The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo
    • Schindler T, Graumann PL, Perl D, Ma S, Schmid FX & Marahiel MA (1999) The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo. J Biol Chem 274: 3407-3413.
    • (1999) J Biol Chem , vol.274 , pp. 3407-3413
    • Schindler, T.1    Graumann, P.L.2    Perl, D.3    Ma, S.4    Schmid, F.X.5    Marahiel, M.A.6
  • 32
    • 0027248819 scopus 로고
    • Structure in solution of the major cold-shock protein from Bacillus subtilis
    • Schnuchel A, Wiltscheck R, Czisch M et al. (1993) Structure in solution of the major cold-shock protein from Bacillus subtilis. Nature 364: 169-171.
    • (1993) Nature , vol.364 , pp. 169-171
    • Schnuchel, A.1    Wiltscheck, R.2    Czisch, M.3
  • 33
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding J, Biegert A & Lupas AN (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33: W244-W248.
    • (2005) Nucleic Acids Res , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 34
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura KDJ, Nei M & Kumar S (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.D.J.1    Nei, M.2    Kumar, S.3
  • 35
    • 77951961719 scopus 로고    scopus 로고
    • How significant is a protein structure similarity with TM-score=0.5?
    • Xu J & Zhang Y (2010) How significant is a protein structure similarity with TM-score=0.5? Bioinformatics 26: 889-895.
    • (2010) Bioinformatics , vol.26 , pp. 889-895
    • Xu, J.1    Zhang, Y.2
  • 36
    • 0030856635 scopus 로고    scopus 로고
    • Growth-phase-dependent expression of cspD, encoding a member of the CspA family in Escherichia coli
    • Yamanaka K & Inouye M (1997) Growth-phase-dependent expression of cspD, encoding a member of the CspA family in Escherichia coli. J Bacteriol 179: 5126-5130.
    • (1997) J Bacteriol , vol.179 , pp. 5126-5130
    • Yamanaka, K.1    Inouye, M.2
  • 37
    • 0028236749 scopus 로고
    • Cloning, sequencing, and characterization of multicopy suppressors of a mukB mutation in Escherichia coli
    • Yamanaka K, Mitani T, Ogura T, Niki H & Hiraga S (1994) Cloning, sequencing, and characterization of multicopy suppressors of a mukB mutation in Escherichia coli. Mol Microbiol 13: 301-312.
    • (1994) Mol Microbiol , vol.13 , pp. 301-312
    • Yamanaka, K.1    Mitani, T.2    Ogura, T.3    Niki, H.4    Hiraga, S.5
  • 38
    • 0035057105 scopus 로고    scopus 로고
    • CspD, a novel DNA replication inhibitor induced during the stationary phase in Escherichia coli
    • Yamanaka K, Zheng W, Crooke E, Wang YH & Inouye M (2001) CspD, a novel DNA replication inhibitor induced during the stationary phase in Escherichia coli. Mol Microbiol 39: 1572-1584.
    • (2001) Mol Microbiol , vol.39 , pp. 1572-1584
    • Yamanaka, K.1    Zheng, W.2    Crooke, E.3    Wang, Y.H.4    Inouye, M.5
  • 39
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: a protein structure alignment algorithm based on the TM-score
    • Zhang Y & Skolnick J (2005) TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res 33: 2302-2309.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.