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Volumn 269, Issue 4, 1997, Pages 514-528

The quaternary geometry of transcription termination factor rho: Assignment by chemical cross-linking

Author keywords

Chemical cross linking; Hexameric ATPase; Quaternary geometry; Rho factor; Transcription termination

Indexed keywords

ADIPIMIDIC ACID DIMETHYL ESTER; DIMER; GLUTARIC ACID; NITROBENZENE DERIVATIVE; PROTEIN SUBUNIT; RHO FACTOR; SUBERIMIDIC ACID DIMETHYL ESTER; SUCCINIMIDE DERIVATIVE; TARTARIC ACID;

EID: 0031580197     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1059     Document Type: Article
Times cited : (31)

References (39)
  • 2
    • 0028861610 scopus 로고
    • Cross-linking of porin with glutardialdehyde: A test for the adequacy of premises of cross-linking theory
    • Azem A., Shaked I., Rosenbusch J. P., Daniel E. Cross-linking of porin with glutardialdehyde: a test for the adequacy of premises of cross-linking theory. Biochim. Biophys. Acta. 1243:1995;151-156.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 151-156
    • Azem, A.1    Shaked, I.2    Rosenbusch, J.P.3    Daniel, E.4
  • 4
    • 0023666140 scopus 로고
    • Transcription termination factor rho is an RNA-DNA helicase
    • Brennan C. A., Dombroski A. J., Platt T. Transcription termination factor rho is an RNA-DNA helicase. Cell. 48:1987;945-952.
    • (1987) Cell , vol.48 , pp. 945-952
    • Brennan, C.A.1    Dombroski, A.J.2    Platt, T.3
  • 5
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides toEscherichia coli
    • Bujalowski W., Klonowska M. M. Negative cooperativity in the binding of nucleotides toEscherichia coli. Biochemistry. 32:1993;5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 6
    • 0023986585 scopus 로고
    • Structure of rho factor: An RNA-binding domain and a separate region with strong similarity to proven ATP-binding domains
    • Dombroski A. J., Platt T. Structure of rho factor: an RNA-binding domain and a separate region with strong similarity to proven ATP-binding domains. Proc. Natl Acad. Sci. USA. 85:1988;2538-2542.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2538-2542
    • Dombroski, A.J.1    Platt, T.2
  • 7
    • 0024270328 scopus 로고
    • Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor
    • Dombroski A. J., Brennan C. A., Spear P., Platt T. Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor. J. Biol. Chem. 263:1988a;18802-18809.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18802-18809
    • Dombroski, A.J.1    Brennan, C.A.2    Spear, P.3    Platt, T.4
  • 8
    • 0024289518 scopus 로고
    • The ATP binding site on rho protein. Affinity labeling of Lys181 by pyridoxal 5′-diphospho-5′-adenosine
    • Dombroski A. J., LaDine J. R., Cross R. L., Platt T. The ATP binding site on rho protein. Affinity labeling of Lys181 by pyridoxal 5′-diphospho-5′-adenosine. J. Biol. Chem. 263:1988b;18810-18815.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18810-18815
    • Dombroski, A.J.1    LaDine, J.R.2    Cross, R.L.3    Platt, T.4
  • 9
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • Dong F., Gogol E. P., von Hippel P. H. The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J. Biol. Chem. 270:1995;7462-7473.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 10
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman E. H., Yu X., Wild R., Hingorani M. M., Patel S. S. Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl Acad. Sci. USA. 92:1995;3869-3873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 11
    • 0019975812 scopus 로고
    • Stabilization of the hexameric form ofEscherichia coli
    • Finger L. R., Richardson J. P. Stabilization of the hexameric form ofEscherichia coli. J. Mol. Biol. 156:1982;203-219.
    • (1982) J. Mol. Biol. , vol.156 , pp. 203-219
    • Finger, L.R.1    Richardson, J.P.2
  • 12
    • 0019325218 scopus 로고
    • ATP-induced changes in the binding of RNA synthesis termination protein rho to RNA
    • Galluppi G. R., Richardson J. P. ATP-induced changes in the binding of RNA synthesis termination protein rho to RNA. J. Mol. Biol. 138:1980;513-539.
    • (1980) J. Mol. Biol. , vol.138 , pp. 513-539
    • Galluppi, G.R.1    Richardson, J.P.2
  • 13
    • 0027049248 scopus 로고
    • Functional interactions of ligand cofactors withEscherichia coli
    • Geiselmann J., von Hippel P. H. Functional interactions of ligand cofactors withEscherichia coli. Protein Sci. 1:1992;850-860.
    • (1992) Protein Sci. , vol.1 , pp. 850-860
    • Geiselmann, J.1    Von Hippel, P.H.2
  • 16
  • 17
    • 0017079854 scopus 로고
    • Crosslinking with bifunctional reagents as a means for studying the symmetry of oligomeric proteins
    • Hajdu J., Bartha F., Friedrich P. Crosslinking with bifunctional reagents as a means for studying the symmetry of oligomeric proteins. Eur. J. Biochem. 68:1976;373-383.
    • (1976) Eur. J. Biochem. , vol.68 , pp. 373-383
    • Hajdu, J.1    Bartha, F.2    Friedrich, P.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0017582694 scopus 로고
    • Characterization of the nucleotide triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor rho. I. Enzymatic properties and effects of inhibitors
    • Lowery C., Richardson J. P. Characterization of the nucleotide triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor rho. I. Enzymatic properties and effects of inhibitors. J. Biol. Chem. 252:1977a;1375-1380.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1375-1380
    • Lowery, C.1    Richardson, J.P.2
  • 20
    • 0017579916 scopus 로고
    • Characterization of the nucleotide triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor rho. II. Influence of synthetic RNA homopolymers and random copolymers on the reaction
    • Lowery C., Richardson J. P. Characterization of the nucleotide triphosphate phosphohydrolase (ATPase) activity of RNA synthesis termination factor rho. II. Influence of synthetic RNA homopolymers and random copolymers on the reaction. J. Biol. Chem. 252:1977b;1381-1385.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1381-1385
    • Lowery, C.1    Richardson, J.P.2
  • 21
    • 0029565119 scopus 로고
    • Structural and functional dissections of transcription termination factor rho by random mutagenesis
    • Miwa Y., Horiguchi T., Shigesada K. Structural and functional dissections of transcription termination factor rho by random mutagenesis. J. Mol. Biol. 254:1995;815-837.
    • (1995) J. Mol. Biol. , vol.254 , pp. 815-837
    • Miwa, Y.1    Horiguchi, T.2    Shigesada, K.3
  • 22
    • 0015527720 scopus 로고
    • Observations on the structure of the termination factor rho and its attachment to DNA
    • Oda T., Takanami M. Observations on the structure of the termination factor rho and its attachment to DNA. J. Mol. Biol. 71:1972;799-802.
    • (1972) J. Mol. Biol. , vol.71 , pp. 799-802
    • Oda, T.1    Takanami, M.2
  • 23
    • 0028943365 scopus 로고
    • Nucleotide binding studies of bacteriophage T7 DNA helicase-primase protein
    • Patel S. S., Hingorani M. M. Nucleotide binding studies of bacteriophage T7 DNA helicase-primase protein. Biophys. J. 68:1995;186s-190s.
    • (1995) Biophys. J. , vol.68
    • Patel, S.S.1    Hingorani, M.M.2
  • 24
    • 0021100910 scopus 로고
    • The nucleotide sequence of the rho gene of E. coli
    • Pinkham J. L., Platt T. The nucleotide sequence of the rho gene of E. coli. Nucl. Acids Res. 11:1983;3531-3545.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 3531-3545
    • Pinkham, J.L.1    Platt, T.2
  • 25
    • 0002454433 scopus 로고
    • Escherichia coli
    • Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Platt T., Richardson J. P. Escherichia coli. Transriptional Regulation. 1992;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1992) Transriptional Regulation
    • Platt, T.1    Richardson, J.P.2
  • 26
    • 0030053611 scopus 로고    scopus 로고
    • Structural organization of transcription termination factor rho
    • Richardson J. P. Structural organization of transcription termination factor rho. J. Biol. Chem. 271:1996;1251-1254.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1251-1254
    • Richardson, J.P.1
  • 27
    • 0019315373 scopus 로고
    • Ribonucleic acid release activity of transcription termination protein rho is dependent on the hydrolysis of nucleoside triphosphates
    • Richardson J. P., Conaway R. Ribonucleic acid release activity of transcription termination protein rho is dependent on the hydrolysis of nucleoside triphosphates. Biochemistry. 19:1980;4293-4299.
    • (1980) Biochemistry , vol.19 , pp. 4293-4299
    • Richardson, J.P.1    Conaway, R.2
  • 28
    • 0029831394 scopus 로고    scopus 로고
    • Rho-dependent termination of transcription is governed primarily by the upstream rho utilization (rut
    • Richardson L. V., Richardson J. P. Rho-dependent termination of transcription is governed primarily by the upstream rho utilization (rut. J. Biol. Chem. 271:1996;21597-21603.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21597-21603
    • Richardson, L.V.1    Richardson, J.P.2
  • 29
    • 0014685875 scopus 로고
    • Termination factor for RNA synthesis
    • Roberts J. W. Termination factor for RNA synthesis. Nature. 224:1969;1168-1174.
    • (1969) Nature , vol.224 , pp. 1168-1174
    • Roberts, J.W.1
  • 31
    • 0026486730 scopus 로고
    • ATPase activity of transcription-termination factor rho: Functional dimer model
    • Seifried S. E., Easton J. B., von Hippel P. H. ATPase activity of transcription-termination factor rho: functional dimer model. Proc. Natl Acad. Sci. USA. 89:1992;10454-10458.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10454-10458
    • Seifried, S.E.1    Easton, J.B.2    Von Hippel, P.H.3
  • 32
    • 0018958616 scopus 로고
    • Studies of RNA release reaction catalyzed by E. coli
    • Shigesada K., Wu C.-W. Studies of RNA release reaction catalyzed byE. coli. Nucl. Acids Res. 8:1980;3355-3369.
    • (1980) Nucl. Acids Res. , vol.8 , pp. 3355-3369
    • Shigesada, K.1    Wu, C.-W.2
  • 34
    • 0027976995 scopus 로고
    • Evidence supporting a tethered tracking model for helicase activity ofEscherichia coli
    • Steinmetz E. J., Platt T. Evidence supporting a tethered tracking model for helicase activity ofEscherichia coli. Proc. Natl Acad. Sci. USA. 91:1994;1401-1405.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1401-1405
    • Steinmetz, E.J.1    Platt, T.2
  • 35
    • 0023770755 scopus 로고
    • Escherichia coli
    • Stitt B. L. Escherichia coli. J. Biol. Chem. 263:1988;11130-11137.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11130-11137
    • Stitt, B.L.1
  • 38
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:1969;4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2


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