scholarly journals Non-Watson-Crick interactions between PNA and DNA inhibit the ATPase activity of bacteriophage T4 Dda helicase

2002 ◽  
Vol 30 (4) ◽  
pp. 950-957 ◽  
Author(s):  
A. J. Tackett
Keyword(s):  
Atpase Activity ◽  
Bacteriophage T4 ◽  
Bacteriophage T4 Dda Helicase

scholarly journals Evidence for a Functional Monomeric Form of the Bacteriophage T4 Dda Helicase

2001 ◽  
Vol 276 (23) ◽  
pp. 19691-19698 ◽  
Author(s):  
Patrick D. Morris ◽  
Alan J. Tackett ◽  
Kirk Babb ◽  
Bindu Nanduri ◽  
Chris Chick ◽  
...  
Keyword(s):  
Bacteriophage T4 ◽  
Monomeric Form ◽  
Bacteriophage T4 Dda Helicase

scholarly journals Pre-steady-state DNA unwinding by bacteriophage T4 Dda helicase reveals a monomeric molecular motor

2002 ◽  
Vol 99 (23) ◽  
pp. 14722-14727 ◽  
Author(s):  
B. Nanduri ◽  
A. K. Byrd ◽  
R. L. Eoff ◽  
A. J. Tackett ◽  
K. D. Raney
Keyword(s):  
Steady State ◽  
Molecular Motor ◽  
Bacteriophage T4 ◽  
Dna Unwinding ◽  
Bacteriophage T4 Dda Helicase

Head Size and DNA Content in Bacteriophage T4

1972 ◽  
Vol 30 ◽  
pp. 200-201
Author(s):  
Fred Eiserling ◽  
A. H. Doermann ◽  
Linde Boehner
Keyword(s):  
Electron Microscopy ◽  
Dna Content ◽  
Bacteriophage T4 ◽  
Head Size ◽  
Virus Particles ◽  
Altered Protein ◽  
A Cell ◽  
Bacterial Viruses ◽  
A Site ◽  
Protein Shell

The control of form or shape inheritance can be approached by studying the morphogenesis of bacterial viruses. Shape variants of bacteriophage T4 with altered protein shell (capsid) size and nucleic acid (DNA) content have been found by electron microscopy, and a mutant (E920g in gene 66) controlling head size has been described. This mutant produces short-headed particles which contain 2/3 the normal DNA content and which are non-viable when only one particle infects a cell (Fig. 1).We report here the isolation of a new mutant (191c) which also appears to be in gene 66 but at a site distinct from E920g. The most striking phenotype of the mutant is the production of about 10% of the phage yield as “giant” virus particles, from 3 to 8 times longer than normal phage (Fig. 2).

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

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