scholarly journals Dualities in the analysis of phage DNA packaging motors

Bacteriophage ◽  
2012 ◽  
Vol 2 (4) ◽  
pp. e23829 ◽  
Author(s):  
Philip Serwer ◽  
Wen Jiang
Keyword(s):  
Dna Packaging ◽  
Phage Dna

Phage DNA packaging

2003 ◽  
Vol 2 (9) ◽  
pp. 537-545 ◽  
Author(s):  
Hisao Fujisawa ◽  
Miyo Morita
Keyword(s):  
Dna Packaging ◽  
Phage Dna

scholarly journals Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy

2017 ◽  
Vol 114 (14) ◽  
pp. 3601-3606 ◽  
Author(s):  
Haiyan Zhao ◽  
Kunpeng Li ◽  
Anna Y. Lynn ◽  
Keith E. Aron ◽  
Guimei Yu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Noncovalent Interactions ◽  
Dna Packaging ◽  
Protein Subunits ◽  
Significant Strength ◽  
Phage Dna ◽  
Mortise And Tenon ◽  
Α Helix ◽  
Β Sheet ◽  
Protein Shell

The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as ∼50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 Å resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon–like intercapsomer joints, and abundant β-sheet–like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic α–helix-to-β–strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.

scholarly journals Testing a proposed paradigm shift in analysis of phage DNA packaging

Bacteriophage ◽  
2016 ◽  
Vol 6 (4) ◽  
pp. e1268664 ◽  
Author(s):  
Philip Serwer ◽  
Elena T. Wright
Keyword(s):  
Paradigm Shift ◽  
Dna Packaging ◽  
Phage Dna

scholarly journals HNH proteins are a widespread component of phage DNA packaging machines

2014 ◽  
Vol 111 (16) ◽  
pp. 6022-6027 ◽  
Author(s):  
S. Kala ◽  
N. Cumby ◽  
P. D. Sadowski ◽  
B. Z. Hyder ◽  
V. Kanelis ◽  
...  
Keyword(s):  
Dna Packaging ◽  
Phage Dna

Replication of Bacteriophage 186 DNA

1972 ◽  
Vol 30 ◽  
pp. 194-195
Author(s):  
Dhruba K. Chattoraj ◽  
Ross B. Inman
Keyword(s):  
Electron Microscopy ◽  
Dna Replication ◽  
Frame Of Reference ◽  
Dna Molecules ◽  
E Coli ◽  
Phage Dna ◽  
Partial Denaturation

Electron microscopy of replicating intermediates has been quite useful in understanding the mechanism of DNA replication in DNA molecules of bacteriophage, mitochondria and plasmids. The use of partial denaturation mapping has made the tool more powerful by providing a frame of reference by which the position of the replicating forks in bacteriophage DNA can be determined on the circular replicating molecules. This provided an easy means to find the origin and direction of replication in λ and P2 phage DNA molecules. DNA of temperate E. coli phage 186 was found to have an unique denaturation map and encouraged us to look into its mode of replication.

Three-Dimensional Structure of Cloned T3 Connector Protein at 1.6nm Resolution

1990 ◽  
Vol 48 (1) ◽  
pp. 282-283
Author(s):  
José L. Carrascosa ◽  
José M. Valpuesta ◽  
Hisao Fujisawa
Keyword(s):  
Dna Sequences ◽  
Expression Vector ◽  
Three Dimensional ◽  
Deae Cellulose ◽  
Dna Packaging ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
Freezing And Thawing ◽  
Three Dimensional Structure ◽  
Dimensional Reconstruction

The head to tail connector of bacteriophages plays a fundamental role in the assembly of viral heads and DNA packaging. In spite of the absence of sequence homology, the structure of connectors from different viruses (T4, Ø29, T3, P22, etc) share common morphological features, that are most clearly revealed in their three-dimensional structure. We have studied the three-dimensional reconstruction of the connector protein from phage T3 (gp 8) from tilted view of two dimensional crystals obtained from this protein after cloning and purification.DNA sequences including gene 8 from phage T3 were cloned, into Bam Hl-Eco Rl sites down stream of lambda promotor PL, in the expression vector pNT45 under the control of cI857. E R204 (pNT89) cells were incubated at 42°C for 2h, harvested and resuspended in 20 mM Tris HC1 (pH 7.4), 7mM 2 mercaptoethanol, ImM EDTA. The cells were lysed by freezing and thawing in the presence of lysozyme (lmg/ml) and ligthly sonicated. The low speed supernatant was precipitated by ammonium sulfate (60% saturated) and dissolved in the original buffer to be subjected to gel nitration through Sepharose 6B, followed by phosphocellulose colum (Pll) and DEAE cellulose colum (DE52). Purified gp8 appeared at 0.3M NaCl and formed crystals when its concentration increased above 1.5 mg/ml.

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