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Science 8 May 1987:
Vol. 236. no. 4802, pp. 690 - 694
DOI: 10.1126/science.3107124
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Articles

Science, Vol 236, Issue 4802, 690-694
Copyright © 1987 by American Association for the Advancement of Science

articles

A small viral RNA is required for in vitro packaging of bacteriophage phi 29 DNA

PX Guo, S Erickson, and D Anderson

A small RNA of Bacillus subtilis bacteriophage phi 29 is shown to have a novel and essential role in viral DNA packaging in vitro. This requirement for RNA in the encapsidation of viral DNA provides a new dimension of complexity to the attendant protein-DNA interactions. The RNA is a constituent of the viral precursor shell of the DNA-packaging machine but is not a component of the mature virion. Studies of the sequential interactions involving this RNA molecule are likely to provide new insight into the structural and possible catalytic roles of small RNA molecules. The phi 29 assembly in extracts and phi 29 DNA packaging in the defined in vitro system were strongly inhibited by treatment with the ribonucleases A or T1. However, phage assembly occurred normally in the presence of ribonuclease A that had been treated with a ribonuclease inhibitor. An RNA of approximately 120 nucleotides co-purified with the phi 29 precursor protein shell (prohead), and this particle was the target of ribonuclease action. Removal of RNA from the prohead by ribonuclease rendered it inactive for DNA packaging. By RNA-DNA hybridization analysis, the RNA was shown to originate from a viral DNA segment very near the left end of the genome, the end packaged first during in vitro assembly.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Complete Genome of the Broad-Host-Range Erwinia amylovora Phage {Phi}Ea21-4 and Its Relationship to Salmonella Phage Felix O1.
S. M. Lehman, A. M. Kropinski, A. J. Castle, and A. M. Svircev (2009)
Appl. Envir. Microbiol. 75, 2139-2147
   Abstract »    Full Text »    PDF »
Novel mechanism of hexamer ring assembly in protein/RNA interactions revealed by single molecule imaging.
F. Xiao, H. Zhang, and P. Guo (2008)
Nucleic Acids Res. 36, 6620-6632
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Characterization and Genomic Analysis of Phage ascc{phi}28, a Phage of the Family Podoviridae Infecting Lactococcus lactis.
S. E. Kotsonis, I. B. Powell, C. J. Pillidge, G. K. Y. Limsowtin, A. J. Hillier, and B. E. Davidson (2008)
Appl. Envir. Microbiol. 74, 3453-3460
   Abstract »    Full Text »    PDF »
Analysis of intermolecular base pair formation of prohead RNA of the phage o29 DNA packaging motor using NMR spectroscopy.
A. Kitamura, P. J. Jardine, D. L. Anderson, S. Grimes, and H. Matsuo (2008)
Nucleic Acids Res. 36, 839-848
   Abstract »    Full Text »    PDF »
Efficient DNA Packaging of Bacteriophage PRD1 Requires the Unique Vertex Protein P6.
N. J. Karhu, G. Ziedaite, D. H. Bamford, and J. K. H. Bamford (2007)
J. Virol. 81, 2970-2979
   Abstract »    Full Text »    PDF »
Controlling bacteriophage phi29 DNA-packaging motor by addition or discharge of a peptide at N-terminus of connector protein that interacts with pRNA.
J. Sun, Y. Cai, W.-D. Moll, and P. Guo (2006)
Nucleic Acids Res. 34, 5482-5490
   Abstract »    Full Text »    PDF »
Controlling RNA self-assembly to form filaments.
L. Nasalean, S. Baudrey, N. B. Leontis, and L. Jaeger (2006)
Nucleic Acids Res. 34, 1381-1392
   Abstract »    Full Text »    PDF »
Affinity of molecular interactions in the bacteriophage {varphi}29 DNA packaging motor..
M. A. Robinson, J. P.A. Wood, S. A. Capaldi, A. J. Baron, C. Gell, D. A. Smith, and N. J. Stonehouse (2006)
Nucleic Acids Res. 34, 2698-2709
   Abstract »    Full Text »    PDF »
Binding of pRNA to the N-terminal 14 amino acids of connector protein of bacteriophage phi29.
F. Xiao, W.-D. Moll, S. Guo, and P. Guo (2005)
Nucleic Acids Res. 33, 2640-2649
   Abstract »    Full Text »    PDF »
Bacillus subtilis Bacteriophage SPP1 DNA Packaging Motor Requires Terminase and Portal Proteins.
A. G. Camacho, A. Gual, R. Lurz, P. Tavares, and J. C. Alonso (2003)
J. Biol. Chem. 278, 23251-23259
   Abstract »    Full Text »    PDF »
The Unique Vertex of Bacterial Virus PRD1 Is Connected to the Viral Internal Membrane.
N. J. Stromsten, D. H. Bamford, and J. K. H. Bamford (2003)
J. Virol. 77, 6314-6321
   Abstract »    Full Text »    PDF »
A Viral RNA That Binds ATP and Contains a Motif Similar to an ATP-binding Aptamer from SELEX.
D. Shu and P. Guo (2003)
J. Biol. Chem. 278, 7119-7125
   Abstract »    Full Text »    PDF »
Computer Modeling of Three-dimensional Structure of DNA-packaging RNA (pRNA) Monomer, Dimer, and Hexamer of Phi29 DNA Packaging Motor.
S. Hoeprich and P. Guo (2002)
J. Biol. Chem. 277, 20794-20803
   Abstract »    Full Text »    PDF »
Purification and functional characterization of p16, the ATPase of the bacteriophage {Phi}29 packaging machinery.
B. Ibarra, J. M. Valpuesta, and J. L. Carrascosa (2001)
Nucleic Acids Res. 29, 4264-4273
   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 »
Mapping the Inter-RNA Interaction of Bacterial Virus Phi29 Packaging RNA by Site-specific Photoaffinity Cross-linking.
K. Garver and P. Guo (2000)
J. Biol. Chem. 275, 2817-2824
   Abstract »    Full Text »    PDF »
In Vitro Selection of Bacteriophage phi 29 Prohead RNA Aptamers for Prohead Binding.
F. Zhang and D. Anderson (1998)
J. Biol. Chem. 273, 2947-2953
   Abstract »    Full Text »    PDF »
Three-dimensional Interaction of Phi29 pRNA Dimer Probed by Chemical Modification Interference, Cryo-AFM, and Cross-linking.
Y. Mat-Arip, K. Garver, C. Chen, S. Sheng, Z. Shao, and P. Guo (2001)
J. Biol. Chem. 276, 32575-32584
   Abstract »    Full Text »    PDF »
A Dimer as a Building Block in Assembling RNA. A HEXAMER THAT GEARS BACTERIAL VIRUS phi29 DNA-TRANSLOCATING MACHINERY.
C. Chen, S. Sheng, Z. Shao, and P. Guo (2000)
J. Biol. Chem. 275, 17510-17516
   Abstract »    Full Text »    PDF »


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