메뉴 건너뛰기




Volumn 192, Issue 12, 2010, Pages 3222-3226

Self-assembly of the bacterial cytoskeleton-associated RNA helicase B protein into polymeric filamentous structures

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; RNA HELICASE; DEAD BOX PROTEIN; ESCHERICHIA COLI PROTEIN; RHLB PROTEIN, E COLI;

EID: 77953985369     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00105-10     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 38849114991 scopus 로고    scopus 로고
    • Polymerization properties of the Thermotoga maritimactin MreB: Roles of temperature, nucleotides, and ions
    • Bean, G. J., and K. J. Amann. 2008. Polymerization properties of the Thermotoga maritimactin MreB: roles of temperature, nucleotides, and ions. Biochemistry. 47:826-835.
    • (2008) Biochemistry , vol.47 , pp. 826-835
    • Bean, G.J.1    Amann, K.J.2
  • 2
    • 0025241323 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Carlier, M. F. 1990. Actin polymerization and ATP hydrolysis. Adv. Biophys. 26:51-73.
    • (1990) Adv. Biophys. , vol.26 , pp. 51-73
    • Carlier, M.F.1
  • 3
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: An mRNA-degrading machine assembled on RNase E
    • Carpousis, A. J. 2007. The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu. Rev. Microbiol. 61:71-87.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 4
    • 0028269435 scopus 로고
    • Copurification of E. coli RNase E and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation
    • Carpousis, A. J., G. Van Houwe, C. Ehretsmann, and H. M. Krisch. 1994. Copurification of E. coli RNase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. Cell 76:889-900.
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 5
    • 13244278205 scopus 로고    scopus 로고
    • The assembly of MreB, a prokaryotic homolog of actin
    • Esue, O., M. Cordero, D. Wirtz, and Y. Tseng. 2005. The assembly of MreB, a prokaryotic homolog of actin. J. Biol. Chem. 280:2628-2635.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2628-2635
    • Esue, O.1    Cordero, M.2    Wirtz, D.3    Tseng, Y.4
  • 6
    • 0037076380 scopus 로고    scopus 로고
    • Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
    • Hu, Z., E. P. Gogol, and J. Lutkenhaus. 2002. Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc. Natl. Acad. Sci. U. S. A. 99:6761-6766.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6761-6766
    • Hu, Z.1    Gogol, E.P.2    Lutkenhaus, J.3
  • 7
    • 0025943266 scopus 로고
    • RhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a prokaryote
    • Kalman, M., H. Murphy, and M. Cashel. 1991. rhlB, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a prokaryote. New Biol. 3:886-895.
    • (1991) New Biol. , vol.3 , pp. 886-895
    • Kalman, M.1    Murphy, H.2    Cashel, M.3
  • 8
    • 28044439868 scopus 로고    scopus 로고
    • RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex
    • Lin, P. H., and S. Lin-Chao. 2005. RhlB helicase rather than enolase is the beta-subunit of the Escherichia coli polynucleotide phosphorylase (PNPase)-exoribonucleolytic complex. Proc. Natl. Acad. Sci. U. S. A. 102:16590-16595.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16590-16595
    • Lin, P.H.1    Lin-Chao, S.2
  • 9
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou, G. G., H. Y. Chang, C. S. Lin, and S. Lin-Chao. 2002. DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J. Biol. Chem. 277:41157-41162.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41157-41162
    • Liou, G.G.1    Chang, H.Y.2    Lin, C.S.3    Lin-Chao, S.4
  • 10
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu, F., A. Putnam, and E. Jankowsky. 2008. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl. Acad. Sci. U. S. A. 105:20209-20214.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 11
    • 0037495314 scopus 로고    scopus 로고
    • 2+-induced FtsZ sheets
    • 2+-induced FtsZ sheets. EMBO J. 18:2364-2367.
    • (1999) EMBO J. , vol.18 , pp. 2364-2367
    • Löwe, J.1    Amos, L.A.2
  • 12
    • 10344248919 scopus 로고    scopus 로고
    • FtsZ fiber bundling is triggered by a conformational change in bound GTP
    • Marrington, R., E. Small, A. Rodger, T. R. Dafforn, and S. G. Addinall. 2004. FtsZ fiber bundling is triggered by a conformational change in bound GTP. J. Biol. Chem. 279:48821-48829.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48821-48829
    • Marrington, R.1    Small, E.2    Rodger, A.3    Dafforn, T.R.4    Addinall, S.G.5
  • 13
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • Miczak, A., V. R. Kaberdin, C. L. Wei, and S. Lin-Chao. 1996. Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc. Natl. Acad. Sci. U. S. A. 93:3865-3869.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 14
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee, A., and J. Lutkenhaus. 1999. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J. Bacteriol. 181:823-832. (Pubitemid 29061564)
    • (1999) Journal of Bacteriology , vol.181 , Issue.3 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 15
    • 0027945686 scopus 로고
    • A protein complex mediating mRNA degradation in Escherichia coli
    • Py, B., H. Causton, E. A. Mudd, and C. F. Higgins. 1994. A protein complex mediating mRNA degradation in Escherichia coli. Mol. Microbiol. 14:717-729.
    • (1994) Mol. Microbiol. , vol.14 , pp. 717-729
    • Py, B.1    Causton, H.2    Mudd, E.A.3    Higgins, C.F.4
  • 16
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py, B., C. F. Higgins, H. M. Krisch, and A. J. Carpousis. 1996. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381:169-172.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 17
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story, R. M., H. Li, and J. N. Abelson. 2001. Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc. Natl. Acad. Sci. U. S. A. 98:1465-1470.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 18
    • 0037168644 scopus 로고    scopus 로고
    • Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE
    • Suefuji, K., R. Valluzzi, and D. RayChaudhuri. 2002. Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. Proc. Natl. Acad. Sci. U. S. A. 99:16776-16781.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 16776-16781
    • Suefuji, K.1    Valluzzi, R.2    RayChaudhuri, D.3
  • 19
    • 54249144032 scopus 로고    scopus 로고
    • New insights into the cellular organization of the RNA processing and degradation machinery of Escherichia coli
    • Taghbalout, A., and L. Rothfield. 2008. New insights into the cellular organization of the RNA processing and degradation machinery of Escherichia coli. Mol. Microbiol. 70:780-782.
    • (2008) Mol. Microbiol. , vol.70 , pp. 780-782
    • Taghbalout, A.1    Rothfield, L.2
  • 20
    • 46649086171 scopus 로고    scopus 로고
    • RNase E and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome
    • Taghbalout, A., and L. Rothfield. 2008. RNase E and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome. J. Biol. Chem. 283:13850-13855.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13850-13855
    • Taghbalout, A.1    Rothfield, L.2
  • 21
    • 33846818898 scopus 로고    scopus 로고
    • RNase E and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton
    • Taghbalout, A., and L. Rothfield. 2007. RNase E and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 104:1667-1672.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1667-1672
    • Taghbalout, A.1    Rothfield, L.2
  • 22
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., L. A. Amos, and J. Lowe. 2001. Prokaryotic origin of the actin cytoskeleton. Nature 413:39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 23
    • 0030815131 scopus 로고    scopus 로고
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • 2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J. 16:5455-5463.
    • (1997) EMBO J. , vol.16 , pp. 5455-5463
    • Yu, X.C.1    Margolin, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.