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Science 25 May 1990:
Vol. 248. no. 4958, pp. 1012 - 1016
DOI: 10.1126/science.2111580

Articles

Science, Vol 248, Issue 4958, 1012-1016
Copyright © 1990 by American Association for the Advancement of Science


articles

A novel nucleoprotein complex at a replication origin

M Serrano, M Salas, and JM Hermoso

Centro de Biologia Molecular (CSIC-UAM), Universidad Autonoma, Madrid, Spain.

The viral protein p6, required for the protein-primed initiation of replication of Bacillus subtilis phage phi 29, forms a nucleoprotein complex at the viral replication origins that shows novel features. Deoxyribonuclease I and hydroxyl radical footprinting data, as well as the induction of positive supercoiling, support a model in which a DNA right-handed superhelix tightly wraps around a multimeric p6 core. The interaction occurs through the DNA minor groove. The activity of p6 not only requires the formation of the complex but also its correct positioning, indicating that the other proteins involved in the initiation of replication recognize, at a precise position, either the p6 core or the DNA conformational change induced by p6.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Involvement of phage {phi}29 DNA polymerase and terminal protein subdomains in conferring specificity during initiation of protein-primed DNA replication.
P. Perez-Arnaiz, E. Longas, L. Villar, J. M. Lazaro, M. Salas, and M. de Vega (2007)
Nucleic Acids Res. 35, 7061-7073
   Abstract »    Full Text »    PDF »
In Vivo DNA Binding of Bacteriophage GA-1 Protein p6.
M. Alcorlo, M. Salas, and J. M. Hermoso (2007)
J. Bacteriol. 189, 8024-8033
   Abstract »    Full Text »    PDF »
Homologies and Divergences in the Transcription Regulatory System of Two Related Bacillus subtilis Phages.
L. Perez-Lago, M. Salas, and A. Camacho (2005)
J. Bacteriol. 187, 6403-6409
   Abstract »    Full Text »    PDF »
A precise DNA bend angle is essential for the function of the phage {phi}29 transcriptional regulator.
L. Pérez-Lago, M. Salas, and A. Camacho (2005)
Nucleic Acids Res. 33, 126-134
   Abstract »    Full Text »    PDF »
Binding of phage {Phi}29 architectural protein p6 to the viral genome: evidence for topological restriction of the phage linear DNA.
V. Gonzalez-Huici, M. Alcorlo, M. Salas, and J. M. Hermoso (2004)
Nucleic Acids Res. 32, 3493-3502
   Abstract »    Full Text »    PDF »
Genome wide, supercoiling-dependent in vivo binding of a viral protein involved in DNA replication and transcriptional control.
V. Gonzalez-Huici, M. Salas, and J. M. Hermoso (2004)
Nucleic Acids Res. 32, 2306-2314
   Abstract »    Full Text »    PDF »
{phi}29 DNA Polymerase Residue Leu384, Highly Conserved in Motif B of Eukaryotic Type DNA Replicases, Is Involved in Nucleotide Insertion Fidelity.
V. Truniger, J. M. Lazaro, M. de Vega, L. Blanco, and M. Salas (2003)
J. Biol. Chem. 278, 33482-33491
   Abstract »    Full Text »    PDF »
{phi}29 Family of Phages.
W. J. J. Meijer, J. A. Horcajadas, and M. Salas (2001)
Microbiol. Mol. Biol. Rev. 65, 261-287
   Abstract »    Full Text »    PDF »
Pleiotropic Effect of Protein P6 on the Viral Cycle of Bacteriophage phi 29.
A. Camacho and M. Salas (2000)
J. Bacteriol. 182, 6927-6932
   Abstract »    Full Text »
Phage phi 29 Terminal Protein Residues Asn80 and Tyr82 Are Recognition Elements of the Replication Origins.
B. Illana, J. M. Lazaro, C. Gutierrez, W. J. J. Meijer, L. Blanco, and M. Salas (1999)
J. Biol. Chem. 274, 15073-15079
   Abstract »    Full Text »    PDF »
Repression of Transcription Initiation in Bacteria.
F. Rojo (1999)
J. Bacteriol. 181, 2987-2991
   Full Text »
Activation of Replication Origins in phi 29-related Phages Requires the Recognition of Initiation Proteins to Specific Nucleoprotein Complexes.
R. Freire, M. Serrano, M. Salas, and J. M. Hermoso (1996)
J. Biol. Chem. 271, 31000-31007
   Abstract »    Full Text »    PDF »
Identification of Residues within Two Regions Involved in Self-association of Viral Histone-like Protein p6 from Phage O29.
A. M. Abril, M. Salas, and J. M. Hermoso (2000)
J. Biol. Chem. 275, 26404-26410
   Abstract »    Full Text »    PDF »
The RepE Initiator Is a Double-stranded and Single-stranded DNA-binding Protein That Forms an Atypical Open Complex at the Onset of Replication of Plasmid pAMbeta 1 from Gram-positive Bacteria.
E. Le Chatelier, L. Janniere, S. D. Ehrlich, and D. Canceill (2001)
J. Biol. Chem. 276, 10234-10246
   Abstract »    Full Text »    PDF »
Repression of Bacteriophage phi 29 Early Promoter C2 by Viral Protein p6 Is Due to Impairment of Closed Complex.
A. Camacho and M. Salas (2001)
J. Biol. Chem. 276, 28927-28932
   Abstract »    Full Text »    PDF »



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Science. ISSN 0036-8075 (print), 1095-9203 (online)