Kinetic characterization of the ATPase activity of the DNA packaging enzyme from bacteriophage .lambda.

Biochemistry ◽  
1993 ◽  
Vol 32 (45) ◽  
pp. 11992-11997 ◽  
Author(s):  
Mary Ann Tomka ◽  
Carlos Enrique Catalano
Keyword(s):  
Atpase Activity ◽  
Bacteriophage Lambda ◽  
Dna Packaging ◽  
Kinetic Characterization ◽  
Dna Packaging Enzyme

A Kinetic Characterization of (Na+, K+)-ATPase Activity in the Gills of the Pelagic Seabob Shrimp Xiphopenaeus kroyeri (Decapoda, Penaeidae)

2014 ◽  
Vol 248 (2) ◽  
pp. 257-272 ◽  
Author(s):  
Francisco Assis Leone ◽  
Malson Neilson Lucena ◽  
Luciana Augusto Rezende ◽  
Daniela Pereira Garçon ◽  
Marcelo Rodrigues Pinto ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Kinetic Characterization ◽  
Xiphopenaeus Kroyeri

Kinetic Characterization of Anticarsia gemmatalis Digestive Serine- Proteases and the Inhibitory Effect of Synthetic Peptides

2018 ◽  
Vol 24 (11) ◽  
Author(s):  
Adriana M. Patarroyo-Vargas ◽  
Yaremis B. Merino-Cabrera ◽  
Jose C. Zanuncio ◽  
Francelina Rocha ◽  
Wellington G. Campos ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Serine Proteases ◽  
Inhibitory Effect ◽  
Anticarsia Gemmatalis ◽  
Kinetic Characterization

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

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.

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