Construction of phi29 DNA-Packaging RNA Monomers, Dimers, and Trimers with Variable Sizes and Shapes as Potential Parts for Nanodevices

2003 ◽  
Vol 3 (4) ◽  
pp. 295-302 ◽  
Author(s):  
Dan Shu ◽  
Lisa P. Huang ◽  
Stephen Hoeprich ◽  
Peixuan Guo
Keyword(s):  
Dna Packaging ◽  
Packaging Rna

scholarly journals Chemical Modification Patterns of Active and Inactive as Well as Procapsid-Bound and Unbound DNA-Packaging RNA of Bacterial Virus Phi29

Virology ◽  
2001 ◽  
Vol 281 (2) ◽  
pp. 281-293 ◽  
Author(s):  
Chunlin Zhang ◽  
Mark Trottier ◽  
Chaoping Chen ◽  
Peixuan Guo
Keyword(s):  
Chemical Modification ◽  
Dna Packaging ◽  
Bacterial Virus ◽  
Packaging Rna

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.

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

scholarly journals Further tests of a recombination model in which chi removes the RecD subunit from the RecBCD enzyme of Escherichia coli.

Genetics ◽  
1990 ◽  
Vol 126 (3) ◽  
pp. 519-533 ◽  
Author(s):  
F W Stahl ◽  
L C Thomason ◽  
I Siddiqi ◽  
M M Stahl
Keyword(s):  
Escherichia Coli ◽  
Dna Sequence ◽  
Dna Packaging ◽  
Lambda Phage ◽  
Recombination Model ◽  
Phage Types ◽  
Point Of Entry ◽  
Reciprocal Recombination ◽  
Recbcd Enzyme ◽  
Lambda Dna

Abstract When one of two infecting lambda phage types in a replication-blocked cross is chi + and DNA packaging is divorced from the RecBCD-chi interaction, complementary chi-stimulated recombinants are recovered equally in mass lysates only if the chi + parent is in excess in the infecting parental mixture. Otherwise, the chi 0 recombinant is recovered in excess. This observation implies that, along with the chi 0 chromosome, two chi + parent chromosomes are involved in the formation of each chi + recombinant. The trimolecular nature of chi +-stimulated recombination is manifest in recombination between lambda and a plasmid. When lambda recombines with a plasmid via the RecBCD pathway, the resulting chromosome has an enhanced probability of undergoing lambda x lambda recombination in the interval into which the plasmid was incorporated. These two observations support a model in which DNA is degraded by Exo V from cos, the sequence that determines the end of packaged lambda DNA and acts as point of entry for RecBCD enzyme, to chi, the DNA sequence that stimulates the RecBCD enzyme to effect recombination. The model supposes that chi acts by ejecting the RecD subunit from the RecBCD enzyme with two consequences. (1) ExoV activity is blocked leaving a highly recombinagenic, frayed duplex end near chi, and (2) as the enzyme stripped of the RecD subunit travels beyond chi it is competent to catalyze reciprocal recombination.

scholarly journals THE INTERACTION OF cos WITH CHI IS SEPARABLE FROM DNA PACKAGING IN recA-recBC-MEDIATED RECOMBINATION OF BACTERIOPHAGE LAMBDA

Genetics ◽  
1983 ◽  
Vol 104 (4) ◽  
pp. 549-570
Author(s):  
Ichizo Kobayashi ◽  
Mary M Stahl ◽  
David Leach ◽  
Franklin W Stahl
Keyword(s):  
Escherichia Coli ◽  
Bacteriophage Lambda ◽  
Dna Packaging ◽  
Bacteriophage Λ ◽  
Entry Site ◽  
Two Component ◽  
General Recombination

ABSTRACT Chi (5′-GCTGGTGG) is a recombinator in RecA- RecBC-mediated recombination in Escherichia coli. In bacteriophage λ vegetative recombination, Chi is fully active only when it is correctly oriented with respect to cos, the site that defines the ends of the packaged chromosome. Here we demonstrate that packaging from cos is not necessary for this cos-Chi interaction. Our evidence suggests that correctly oriented cos is an activator of Chi. cos, as an activator, is (1) dominant over cos  -, (2) active opposite an extensive heterology, (3) able to interact with Chi only when on the same (cis) chromosome, and (4) able to interact with Chi at distances as far as ≥ 20 kb. Thus, cos and Chi form a two-component recombinator system for general recombination. cos may serve as an asymmetric entry site for a recombination enzyme that recognizes Chi in an asymmetric way.

scholarly journals A biomechanical mechanism for initiating DNA packaging

2014 ◽  
Vol 42 (19) ◽  
pp. 11921-11927 ◽  
Author(s):  
Haowei Wang ◽  
Samuel Yehoshua ◽  
Sabrina S. Ali ◽  
William Wiley Navarre ◽  
Joshua N. Milstein
Keyword(s):  
Dna Packaging

scholarly journals The C-terminal domain of the bacteriophage T4 terminase docks on the prohead portal clip region during DNA packaging

Virology ◽  
2013 ◽  
Vol 446 (1-2) ◽  
pp. 293-302 ◽  
Author(s):  
Aparna Banerjee Dixit ◽  
Krishanu Ray ◽  
Julie A. Thomas ◽  
Lindsay W. Black
Keyword(s):  
Bacteriophage T4 ◽  
Dna Packaging ◽  
Terminal Domain
Sign in / Sign up

Export Citation Format

Share Document