메뉴 건너뛰기




Volumn 187, Issue 18, 2005, Pages 6430-6442

Positive autoregulation of cI is a dispensable feature of the phage λ gene regulatory circuitry

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; AUTOREGULATION; BACTERIAL GENE; BACTERIOPHAGE; CI GENE; COMPLEX FORMATION; EVOLUTION; GENE CONTROL; GENE EXPRESSION; GENE FUNCTION; GENE MUTATION; GENE REPRESSION; GENETIC TRANSCRIPTION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; QUALITATIVE ANALYSIS;

EID: 24944550880     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.18.6430-6442.2005     Document Type: Article
Times cited : (26)

References (41)
  • 1
    • 4444256116 scopus 로고    scopus 로고
    • Regulatory circuit design and evolution using phage λ
    • Atsumi, S., and J. W. Little. 2004. Regulatory circuit design and evolution using phage λ. Genes Dev. 18:2086-2094.
    • (2004) Genes Dev. , vol.18 , pp. 2086-2094
    • Atsumi, S.1    Little, J.W.2
  • 2
    • 0018782266 scopus 로고
    • Inactivation of prophage λ repressor in vivo
    • Bailone, A., A. Levine, and R. Devoret. 1979. Inactivation of prophage λ repressor in vivo. J. Mol. Biol. 131:553-572.
    • (1979) J. Mol. Biol. , vol.131 , pp. 553-572
    • Bailone, A.1    Levine, A.2    Devoret, R.3
  • 3
    • 17144456808 scopus 로고    scopus 로고
    • Positive feedback in eukaryotic gene networks: Cell differentiation by graded to binary response conversion
    • Becskei, A., B. Séraphin, and L. Serrano. 2001. Positive feedback in eukaryotic gene networks: cell differentiation by graded to binary response conversion. EMBO J. 20:2528-2535.
    • (2001) EMBO J. , vol.20 , pp. 2528-2535
    • Becskei, A.1    Séraphin, B.2    Serrano, L.3
  • 4
    • 0024462398 scopus 로고
    • A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor
    • Bushman, F. D., C. Shang, and M. Ptashne. 1989. A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor. Cell 58:1163-1171.
    • (1989) Cell , vol.58 , pp. 1163-1171
    • Bushman, F.D.1    Shang, C.2    Ptashne, M.3
  • 5
    • 0034687127 scopus 로고    scopus 로고
    • Coupled energetics of lambda ero repressor self-assembly and site-specific DNA operator binding I: Analysis of ero dimerization from nanomolar to micromolar concentrations
    • Darling, P. J., J. M. Holt, and G. K. Ackers. 2000. Coupled energetics of lambda ero repressor self-assembly and site-specific DNA operator binding I: analysis of ero dimerization from nanomolar to micromolar concentrations. Biochemistry 39:11500-11507.
    • (2000) Biochemistry , vol.39 , pp. 11500-11507
    • Darling, P.J.1    Holt, J.M.2    Ackers, G.K.3
  • 7
    • 0034700165 scopus 로고    scopus 로고
    • Mechanism for a transcriptional activator that works at the isomerization step
    • Dove, S. L., F. W. Huang, and A. Hochschild. 2000. Mechanism for a transcriptional activator that works at the isomerization step. Proc. Natl. Acad. Sci. USA 97:13215-13220.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13215-13220
    • Dove, S.L.1    Huang, F.W.2    Hochschild, A.3
  • 8
    • 0002501256 scopus 로고
    • Bacteriophage λ development: Temporal switches and the choice of lysis or lysogeny
    • Echols, H. 1986. Bacteriophage λ development: temporal switches and the choice of lysis or lysogeny. Annu. Rev. Genet. 2:26-30.
    • (1986) Annu. Rev. Genet. , vol.2 , pp. 26-30
    • Echols, H.1
  • 10
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability
    • Ferrell, J. E., Jr. 2002. Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability. Curr. Opin. Cell Biol. 14:140-148.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 140-148
    • Ferrell Jr., J.E.1
  • 11
    • 0020490669 scopus 로고
    • Mechanism of activation of transcription initiation from the lambda PRM promoter
    • Hawley, D. K., and W. R. McClure. 1982. Mechanism of activation of transcription initiation from the lambda PRM promoter. J. Mol. Biol. 157:493-525.
    • (1982) J. Mol. Biol. , vol.157 , pp. 493-525
    • Hawley, D.K.1    McClure, W.R.2
  • 12
    • 0019266971 scopus 로고
    • The lysis-lysogeny decision of phage λ: Explicit programming and responsiveness
    • Herskowitz, I., and D. Hagen. 1980. The lysis-lysogeny decision of phage λ: explicit programming and responsiveness. Annu. Rev. Genet. 14:399-445.
    • (1980) Annu. Rev. Genet. , vol.14 , pp. 399-445
    • Herskowitz, I.1    Hagen, D.2
  • 13
    • 0020713848 scopus 로고
    • Repressor structure and the mechanism of positive control
    • Hochschild, A., N. Irwin, and M. Ptashne. 1983. Repressor structure and the mechanism of positive control. Cell 32:319-325.
    • (1983) Cell , vol.32 , pp. 319-325
    • Hochschild, A.1    Irwin, N.2    Ptashne, M.3
  • 14
    • 0021821711 scopus 로고
    • A cII-dependent promoter is located within the Q gene of bacteriophage lambda
    • Hoopes, B. C., and W. R. McClure. 1985. A cII-dependent promoter is located within the Q gene of bacteriophage lambda. Proc. Natl. Acad. Sic. USA 82:3134-3138.
    • (1985) Proc. Natl. Acad. Sic. USA , vol.82 , pp. 3134-3138
    • Hoopes, B.C.1    McClure, W.R.2
  • 15
    • 0024292486 scopus 로고
    • Characterization of a doubly mutant derivative of the lambda PRM promoter: Effects of mutations on activation of PRM
    • Hwang, J. J., S. Brown, and G. N. Gussin. 1988. Characterization of a doubly mutant derivative of the lambda PRM promoter: effects of mutations on activation of PRM. J. Mol. Biol. 200:695-708.
    • (1988) J. Mol. Biol. , vol.200 , pp. 695-708
    • Hwang, J.J.1    Brown, S.2    Gussin, G.N.3
  • 16
    • 1642441938 scopus 로고    scopus 로고
    • Structure of a ternary transcription activation complex
    • Jain, D., B. E. Nickels, A. Hochschild, and S. A. Darst. 2004. Structure of a ternary transcription activation complex. Mol. Cell 13:45-53.
    • (2004) Mol. Cell , vol.13 , pp. 45-53
    • Jain, D.1    Nickels, B.E.2    Hochschild, A.3    Darst, S.A.4
  • 17
    • 0007208716 scopus 로고
    • Interactions between DNA-bound repressors govern regulation by the λ phage repressor
    • Johnson, A. D., B. J. Meyer, and M. Ptashne. 1979. Interactions between DNA-bound repressors govern regulation by the λ phage repressor. Proc. Natl. Acad. Sci. USA 76:5061-5065.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5061-5065
    • Johnson, A.D.1    Meyer, B.J.2    Ptashne, M.3
  • 20
    • 0028287795 scopus 로고
    • 70 that result in defects in phage lambda repressor-stimulated transcription
    • 70 that result in defects in phage lambda repressor-stimulated transcription. J. Bacteriol. 176:2991-2998.
    • (1994) J. Bacteriol. , vol.176 , pp. 2991-2998
    • Kuldell, N.1    Hochschild, A.2
  • 21
    • 0037418253 scopus 로고    scopus 로고
    • Retroevolution of lambda Cro toward a stable monomer
    • LeFevre, K. R., and M. H. J. Cordes. 2003. Retroevolution of lambda Cro toward a stable monomer. Proc. Natl. Acad. Sci. USA 100:2345-2350.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2345-2350
    • LeFevre, K.R.1    Cordes, M.H.J.2
  • 22
    • 0028197624 scopus 로고
    • Target of the transcriptional activation function of phage lambda cI protein
    • Li, M., H. Moyle, and M. M. Susskind. 1994. Target of the transcriptional activation function of phage lambda cI protein. Science 263:75-77.
    • (1994) Science , vol.263 , pp. 75-77
    • Li, M.1    Moyle, H.2    Susskind, M.M.3
  • 23
    • 0343188817 scopus 로고
    • Autodigestion of IcxA and phage lambda repressors
    • Little, J. W. 1984. Autodigestion of IcxA and phage lambda repressors. Proc. Natl. Acad. Sci. USA 81:1375-1379.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1375-1379
    • Little, J.W.1
  • 24
    • 0021104403 scopus 로고
    • The SOS regulatory system: Control of its state by the level of RecA protease
    • Little, J. W. 1983. The SOS regulatory system: control of its state by the level of RecA protease. J. Mol. Biol. 167:791-808.
    • (1983) J. Mol. Biol. , vol.167 , pp. 791-808
    • Little, J.W.1
  • 25
    • 0027214683 scopus 로고
    • LexA cleavage and other self-processing reactions
    • Little, J. W. 1993. LexA cleavage and other self-processing reactions. J. Bacteriol. 175:4943-4950.
    • (1993) J. Bacteriol. , vol.175 , pp. 4943-4950
    • Little, J.W.1
  • 26
    • 0020316054 scopus 로고
    • The SOS regulatory system of Escherichia coli
    • Little, J. W., and D. W. Mount. 1982. The SOS regulatory system of Escherichia coli. Cell 29:11-22.
    • (1982) Cell , vol.29 , pp. 11-22
    • Little, J.W.1    Mount, D.W.2
  • 27
    • 0033517148 scopus 로고    scopus 로고
    • Robustness of a gene regulatory circuit
    • Little, J. W., D. P. Shepley, and D. W. Wert. 1999. Robustness of a gene regulatory circuit. EMBO J. 18:4299-4307.
    • (1999) EMBO J. , vol.18 , pp. 4299-4307
    • Little, J.W.1    Shepley, D.P.2    Wert, D.W.3
  • 28
    • 0032079401 scopus 로고    scopus 로고
    • The spacing between binding sites controls the mode of cooperative DNA-protein interactions: Implications for evolution of regulatory circuitry
    • Liu, Z., and J. W. Little. 1998. The spacing between binding sites controls the mode of cooperative DNA-protein interactions: implications for evolution of regulatory circuitry. J. Mol. Biol. 278:331-338.
    • (1998) J. Mol. Biol. , vol.278 , pp. 331-338
    • Liu, Z.1    Little, J.W.2
  • 29
    • 1642442717 scopus 로고    scopus 로고
    • Characterizing spontaneous induction of Six encoding phages using a selectable reporter system
    • Livny, J., and D. I. Friedman. 2004. Characterizing spontaneous induction of Six encoding phages using a selectable reporter system. Mol. Microbiol. 51:1691-1704.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1691-1704
    • Livny, J.1    Friedman, D.I.2
  • 30
    • 0032577383 scopus 로고    scopus 로고
    • Mutations affecting cooperative DNA binding of phage HK022 CI repressor
    • Mao, C., and J. W. Little. 1998. Mutations affecting cooperative DNA binding of phage HK022 CI repressor. J. Mol. Biol. 279:31-48.
    • (1998) J. Mol. Biol. , vol.279 , pp. 31-48
    • Mao, C.1    Little, J.W.2
  • 31
    • 0018868527 scopus 로고
    • R) of bacteriophage λ III. λ repressor directly activates gene transcription
    • R) of bacteriophage λ III. λ repressor directly activates gene transcription. J. Mol. Biol. 139:195-205.
    • (1980) J. Mol. Biol. , vol.139 , pp. 195-205
    • Meyer, B.J.1    Ptashne, M.2
  • 32
  • 33
    • 0014945080 scopus 로고
    • Immunity phase-shift in defective lysogens: Non-mutational hereditary change of early regulation of lambda prophage
    • Neubauer, Z., and E. Calef. 1970. Immunity phase-shift in defective lysogens: non-mutational hereditary change of early regulation of lambda prophage. J. Mol. Biol. 51:1-13.
    • (1970) J. Mol. Biol. , vol.51 , pp. 1-13
    • Neubauer, Z.1    Calef, E.2
  • 35
    • 0033545416 scopus 로고    scopus 로고
    • Four dimers of lambda repressor bound to two suitably spaced pairs of lambda operators form octamers and DNA loops over large distances
    • Revet, B., B. Von Wilcken-Bergmann, H. Bessert, A. Barker, and B. Müller-Hill. 1999. Four dimers of lambda repressor bound to two suitably spaced pairs of lambda operators form octamers and DNA loops over large distances. Curr. Biol. 9:151-154.
    • (1999) Curr. Biol. , vol.9 , pp. 151-154
    • Revet, B.1    Von Wilcken-Bergmann, B.2    Bessert, H.3    Barker, A.4    Müller-Hill, B.5
  • 36
    • 0002773599 scopus 로고
    • Lysogenic induction
    • R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.). Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Roberts, J. W., and R. Devoret. 1983. Lysogenic induction, p. 123-144. In R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Lambda 11. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1983) Lambda 11 , pp. 123-144
    • Roberts, J.W.1    Devoret, R.2
  • 38
    • 0017807393 scopus 로고
    • Primary structure of the lambda repressor
    • Sauer, R. T., and R. Anderegg. 1978. Primary structure of the lambda repressor. Biochemistry 17:1092-1100.
    • (1978) Biochemistry , vol.17 , pp. 1092-1100
    • Sauer, R.T.1    Anderegg, R.2
  • 39
    • 0022429106 scopus 로고
    • R control system of bacteriophage lambda: A physical-chemical model for gene regulation
    • R control system of bacteriophage lambda: a physical-chemical model for gene regulation. J. Mol. Biol. 181:211-230.
    • (1985) J. Mol. Biol. , vol.181 , pp. 211-230
    • Shea, M.A.1    Ackers, G.K.2
  • 40
    • 0020668103 scopus 로고
    • Mutations affecting two different steps in transcription initiation at the phage lambda PRM promoter
    • Shih, M. C., and G. N. Gussin. 1983. Mutations affecting two different steps in transcription initiation at the phage lambda PRM promoter. Proc. Natl. Acad. Sci. USA 80:496-500.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 496-500
    • Shih, M.C.1    Gussin, G.N.2
  • 41
    • 0028232652 scopus 로고
    • Specificity determinants for the interaction of λ repressor and P22 repressor dimers
    • Whipple, F. W., N. H. Kuldell, L. A. Cheatham, and A. Hochschild. 1994. Specificity determinants for the interaction of λ repressor and P22 repressor dimers. Genes Dev. 8:1212-1223.
    • (1994) Genes Dev. , vol.8 , pp. 1212-1223
    • Whipple, F.W.1    Kuldell, N.H.2    Cheatham, L.A.3    Hochschild, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.