메뉴 건너뛰기




Volumn 275, Issue 8, 2008, Pages 1835-1851

ATPase activity of RecD is essential for growth of the Antarctic Pseudomonas syringae Lz4W at low temperature

Author keywords

Cold adaptation; Pseudomonas syringae; RecBCD enzyme; RecD ATPase; RecD helicase

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HELICASE; MUTANT PROTEIN; PROTEIN RECD; UNCLASSIFIED DRUG;

EID: 41549087040     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06342.x     Document Type: Article
Times cited : (9)

References (50)
  • 1
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE Koonin EV (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3, 419 429.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 2
    • 0030943197 scopus 로고    scopus 로고
    • The RecD subunit of the RecBCD enzyme from Escherichia coli is a single-stranded DNA-dependent ATPase
    • Chen HW, Ruan B, Yu M, Wang J Julin DA (1997) The RecD subunit of the RecBCD enzyme from Escherichia coli is a single-stranded DNA-dependent ATPase. J Biol Chem, 272, 10072 10079.
    • (1997) J Biol Chem , vol.272 , pp. 10072-10079
    • Chen, H.W.1    Ruan, B.2    Yu, M.3    Wang, J.4    Julin, D.A.5
  • 4
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ
    • Kuzminov A (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ. Microbiol Mol Biol Rev 63, 751 813.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 5
    • 0037698985 scopus 로고    scopus 로고
    • RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity
    • Taylor AF Smith GR (2003) RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature 423, 889 893.
    • (2003) Nature , vol.423 , pp. 889-893
    • Taylor, A.F.1    Smith, G.R.2
  • 6
    • 0021702028 scopus 로고
    • A new class of Escherichia coli recBC mutants: Implications for the role of RecBC enzyme in homologous recombination
    • Chaudhury AM Smith GR (1984) A new class of Escherichia coli recBC mutants: implications for the role of RecBC enzyme in homologous recombination. Proc Natl Acad Sci USA 81, 7850 7854.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7850-7854
    • Chaudhury, A.M.1    Smith, G.R.2
  • 8
    • 0034614654 scopus 로고    scopus 로고
    • A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions
    • Wang J, Chen R Julin DA (2000) A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions. J Biol Chem 275, 507 513.
    • (2000) J Biol Chem , vol.275 , pp. 507-513
    • Wang, J.1    Chen, R.2    Julin, D.A.3
  • 9
    • 27744497422 scopus 로고    scopus 로고
    • Translocation by the RecB motor is an absolute requirement for chi-recognition and RecA protein loading by RecBCD enzyme
    • Spies M, Dillingham MS Kowalczykowski SC (2005) Translocation by the RecB motor is an absolute requirement for chi-recognition and RecA protein loading by RecBCD enzyme. J Biol Chem 280, 37078 37087.
    • (2005) J Biol Chem , vol.280 , pp. 37078-37087
    • Spies, M.1    Dillingham, M.S.2    Kowalczykowski, S.C.3
  • 10
    • 0031788886 scopus 로고    scopus 로고
    • Adaptation to low temperature and regulation of gene expression in Antarctic psychrotrophic bacteria
    • Ray MK, Seshukumar G, Janiyani K, Kannan K, Jagatap P, Basu MK Shivaji S (1998) Adaptation to low temperature and regulation of gene expression in Antarctic psychrotrophic bacteria. J Biosci 23, 423 435.
    • (1998) J Biosci , vol.23 , pp. 423-435
    • Ray, M.K.1    Seshukumar, G.2    Janiyani, K.3    Kannan, K.4    Jagatap, P.5    Basu, M.K.6    Shivaji, S.7
  • 11
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications
    • Russell NJ (1998) Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications. Adv Biochem Eng Biotechnol 61, 1 21.
    • (1998) Adv Biochem Eng Biotechnol , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 12
    • 0040626487 scopus 로고    scopus 로고
    • Cold shock response and low temperature adaptation in psychrotrophic bacteria
    • Hebraud M Potier P (1999) Cold shock response and low temperature adaptation in psychrotrophic bacteria. J Mol Microbiol Biotechnol 1, 211 219.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , pp. 211-219
    • Hebraud, M.1    Potier, P.2
  • 13
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller G Gerday C (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol 1, 200 208.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 14
    • 34447526095 scopus 로고    scopus 로고
    • Exoribonuclease R in Pseudomonas syringae is essential for growth at low temperature and plays a novel role in the 3′ end processing of 16S and 5S ribosomal RNA
    • Purusharth RI, Bollapalli M Ray MK (2007) Exoribonuclease R in Pseudomonas syringae is essential for growth at low temperature and plays a novel role in the 3′ end processing of 16S and 5S ribosomal RNA. J Biol Chem 282, 16267 16277.
    • (2007) J Biol Chem , vol.282 , pp. 16267-16277
    • Purusharth, R.I.1    Bollapalli, M.2    Ray, M.K.3
  • 15
    • 25444473121 scopus 로고    scopus 로고
    • RecD plays an essential function during growth at low temperature in the Antarctic bacterium Pseudomonas syringae Lz4W
    • Regha K, Satapathy AK Ray MK (2005) RecD plays an essential function during growth at low temperature in the Antarctic bacterium Pseudomonas syringae Lz4W. Genetics 170, 1473 1484.
    • (2005) Genetics , vol.170 , pp. 1473-1484
    • Regha, K.1    Satapathy, A.K.2    Ray, M.K.3
  • 16
    • 0032939636 scopus 로고    scopus 로고
    • RecD function is required for high-pressure growth of a deep-sea bacterium
    • Bidle KA Bartlett DH (1999) RecD function is required for high-pressure growth of a deep-sea bacterium. J Bacteriol 181, 2330 2337.
    • (1999) J Bacteriol , vol.181 , pp. 2330-2337
    • Bidle, K.A.1    Bartlett, D.H.2
  • 17
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall MC Matson SW (1999) Helicase motifs: the engine that powers DNA unwinding. Mol Microbiol 34, 867 877.
    • (1999) Mol Microbiol , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 20
    • 0030877168 scopus 로고    scopus 로고
    • Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect
    • Hall MC Matson SW (1997) Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect. J Biol Chem 272, 18614 18620.
    • (1997) J Biol Chem , vol.272 , pp. 18614-18620
    • Hall, M.C.1    Matson, S.W.2
  • 21
    • 0030704250 scopus 로고    scopus 로고
    • Conserved motifs II to VI of DNA helicase II from Escherichia coli are all required for biological activity
    • Zhang G, Deng E, Baugh LR, Hamilton CM, Maples VF Kushner SR (1997) Conserved motifs II to VI of DNA helicase II from Escherichia coli are all required for biological activity. J Bacteriol 179, 7544 7550.
    • (1997) J Bacteriol , vol.179 , pp. 7544-7550
    • Zhang, G.1    Deng, E.2    Baugh, L.R.3    Hamilton, C.M.4    Maples, V.F.5    Kushner, S.R.6
  • 23
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of Esherichia coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S, Hsieh J, Gauss GH, Lohman TM Waksman G (1997) Major domain swiveling revealed by the crystal structures of complexes of Esherichia coli Rep helicase bound to single-stranded DNA and ADP. Cell 90, 635 647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 24
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS Wigley DB (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97, 75 84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 25
    • 0032812570 scopus 로고    scopus 로고
    • A RNA polymerase with transcriptional activity at 0°C from the Antarctic bacterium Pseudomonas syringae
    • Uma S, Jadhav RS, Seshukumar G, Shivaji S Ray MK (1999) A RNA polymerase with transcriptional activity at 0°C from the Antarctic bacterium Pseudomonas syringae. FEBS Lett 453, 313 317.
    • (1999) FEBS Lett , vol.453 , pp. 313-317
    • Uma, S.1    Jadhav, R.S.2    Seshukumar, G.3    Shivaji, S.4    Ray, M.K.5
  • 27
    • 10644241539 scopus 로고    scopus 로고
    • DNA helicase activity of the RecD protein from Deinococcus radiodurans
    • Wang J Julin DA (2004) DNA helicase activity of the RecD protein from Deinococcus radiodurans. J Biol Chem 279, 52024 52032.
    • (2004) J Biol Chem , vol.279 , pp. 52024-52032
    • Wang, J.1    Julin, D.A.2
  • 28
    • 55449115425 scopus 로고    scopus 로고
    • Comparative and evolutionary analysis of the bacterial homologous recombination systems
    • Rocha EPC, Cornet E Michel B (2005) Comparative and evolutionary analysis of the bacterial homologous recombination systems. PLoS Genet 15, 247 259.
    • (2005) PLoS Genet , vol.15 , pp. 247-259
    • Rocha, E.P.C.1    Cornet, E.2    Michel, B.3
  • 29
    • 0031554722 scopus 로고    scopus 로고
    • Biochemical properties of RuvBD113N: A mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities
    • Mezard C, Davies AA, Stasiak A West SC (1997) Biochemical properties of RuvBD113N: a mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities. J Mol Biol 271, 704 717.
    • (1997) J Mol Biol , vol.271 , pp. 704-717
    • Mezard, C.1    Davies, A.A.2    Stasiak, A.3    West, S.C.4
  • 30
    • 0033520395 scopus 로고    scopus 로고
    • Role of Walker motif a of RuvB protein in promoting branch migration of Holliday junctions. Walker motif a mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB
    • Hishida T, Iwasaki H, Yagi T Shinagawa H (1999) Role of Walker motif A of RuvB protein in promoting branch migration of Holliday junctions. Walker motif A mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB. J Biol Chem 274, 25335 25342.
    • (1999) J Biol Chem , vol.274 , pp. 25335-25342
    • Hishida, T.1    Iwasaki, H.2    Yagi, T.3    Shinagawa, H.4
  • 31
    • 0037321633 scopus 로고    scopus 로고
    • Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9
    • Marintcheva B Weller SK (2003) Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9. J Virol 77, 2477 2488.
    • (2003) J Virol , vol.77 , pp. 2477-2488
    • Marintcheva, B.1    Weller, S.K.2
  • 32
    • 0015406320 scopus 로고
    • Uncoupling of the recBC ATPase from DNase by DNA crosslinked with psoralen
    • Karu AE Linn S (1972) Uncoupling of the recBC ATPase from DNase by DNA crosslinked with psoralen. Proc Natl Acad Sci USA 69, 2855 2859.
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2855-2859
    • Karu, A.E.1    Linn, S.2
  • 33
    • 33746867967 scopus 로고    scopus 로고
    • Inhibition of RecBCD enzyme by antineoplastic DNA alkylating agents
    • Dziegielewska B, Beerman TA Bianco PR (2006) Inhibition of RecBCD enzyme by antineoplastic DNA alkylating agents. J Mol Biol 361, 898 919.
    • (2006) J Mol Biol , vol.361 , pp. 898-919
    • Dziegielewska, B.1    Beerman, T.A.2    Bianco, P.R.3
  • 34
    • 0032824138 scopus 로고    scopus 로고
    • Structure-based mutagenesis study of hepatitis C virus NS3 helicase
    • Lin C Kim JL (1999) Structure-based mutagenesis study of hepatitis C virus NS3 helicase. J Virol 73, 8798 8807.
    • (1999) J Virol , vol.73 , pp. 8798-8807
    • Lin, C.1    Kim, J.L.2
  • 35
    • 0031901334 scopus 로고    scopus 로고
    • The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication
    • Gross CH Shuman S (1998) The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication. J Virol 72, 4729 4736.
    • (1998) J Virol , vol.72 , pp. 4729-4736
    • Gross, C.H.1    Shuman, S.2
  • 36
    • 15444357274 scopus 로고    scopus 로고
    • A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo
    • Brosh RM Jr. Matson SW (1997) A point mutation in Escherichia coli DNA helicase II renders the enzyme nonfunctional in two DNA repair pathways. Evidence for initiation of unwinding from a nick in vivo. J Biol Chem 272, 572 579.
    • (1997) J Biol Chem , vol.272 , pp. 572-579
    • Brosh Jr., R.M.1    Matson, S.W.2
  • 37
    • 0032571396 scopus 로고    scopus 로고
    • Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and ssDNA binding activities via conformational changes
    • Hall MC, Ozsoy AZ Matson SW (1998) Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and ssDNA binding activities via conformational changes. J Mol Biol 277, 257 271.
    • (1998) J Mol Biol , vol.277 , pp. 257-271
    • Hall, M.C.1    Ozsoy, A.Z.2    Matson, S.W.3
  • 38
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination dependent replication
    • Kowalczykowski SC (2000) Initiation of genetic recombination and recombination dependent replication. Trends Biochem Sci 25, 156 165.
    • (2000) Trends Biochem Sci , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 39
    • 0035679232 scopus 로고    scopus 로고
    • Recombinational DNA repair of damaged replication forks in Escherichia coli: Questions
    • Cox MM (2001) Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu Rev Genet 35, 53 82.
    • (2001) Annu Rev Genet , vol.35 , pp. 53-82
    • Cox, M.M.1
  • 40
    • 0027288130 scopus 로고
    • Kinetics and processivity of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
    • Korangy F Julin DA (1993) Kinetics and processivity of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli. Biochemistry 32, 4873 4880.
    • (1993) Biochemistry , vol.32 , pp. 4873-4880
    • Korangy, F.1    Julin, D.A.2
  • 41
    • 0032562543 scopus 로고    scopus 로고
    • Functions of the ATP hydrolysis subunits (RecB and RecD) in the nuclease reactions catalyzed by the RecBCD enzyme from Escherichia coli
    • Chen H, Randle DE, Gabbidon M Julin DA (1998) Functions of the ATP hydrolysis subunits (RecB and RecD) in the nuclease reactions catalyzed by the RecBCD enzyme from Escherichia coli. J Mol Biol 278, 89 104.
    • (1998) J Mol Biol , vol.278 , pp. 89-104
    • Chen, H.1    Randle, D.E.2    Gabbidon, M.3    Julin, D.A.4
  • 42
    • 0023790378 scopus 로고
    • The genetic dependence of recombination in recD mutants of Escherichia coli
    • Lovett ST, Luisi-DeLuca C Kolodner RD (1988) The genetic dependence of recombination in recD mutants of Escherichia coli. Genetics 120, 37 45.
    • (1988) Genetics , vol.120 , pp. 37-45
    • Lovett, S.T.1    Luisi-Deluca, C.2    Kolodner, R.D.3
  • 45
    • 0030786334 scopus 로고    scopus 로고
    • A rapid and efficient method for site-directed mutagenesis using one-step overlap extension PCR
    • Urban A, Neukirchen S Jaeger KE (1997) A rapid and efficient method for site-directed mutagenesis using one-step overlap extension PCR. Nucleic Acids Res 25, 2227 2228.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2227-2228
    • Urban, A.1    Neukirchen, S.2    Jaeger, K.E.3
  • 46
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vitro genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon R, Priefer UB Puhler A (1983) A broad host range mobilization system for in vitro genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1, 784 791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.B.2    Puhler, A.3
  • 47
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 48
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM Sternberg MJ (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 299, 499 520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 49
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Suppl
    • Bates PA, Kelley LA, MacCallum RM Sternberg MJ (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins Suppl 5, 39 46.
    • (2001) Proteins , vol.5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4
  • 50
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47, 110 119.
    • (1991) Acta Crystallogr a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.