Purification and properties of the. gamma. -protein specified by bacteriophage lambda: an inhibitor of the host RecBC recombination enzyme
Journal Article
·
· Proc. Natl. Acad. Sci. U.S.A.; (United States)
Previous experiments have indicated that the gam gene of bacteriophage lambda is responsible for an inhibition of the RecBC DNase--an enzyme that is essential for the major host pathway of genetic recombination. We report here experiments that define the inhibitor as the protein product of the gam gene (''..gamma..-protein'') and that characterize the inhibition reaction with highly purified preparations of ..gamma..-protein and RecBC DNase. Genetic characterization was performed with partially purified fractions prepared from cells infected with various lambda mutants. An activity that inhibits RecBC DNase was absent in extracts prepared after infection by phage that carry nonsense or deletion mutations in the gam gene; this activity was highly thermolabile in an extract prepared after infection by phage that carry a temperature-sensitive mutation in the gam gene. For biochemical characterization, the ..gamma..-protein has been purified more than 800-fold. This highly purified preparation inhibited all of the known catalytic activities associated with the RecBC enzyme, but exhibited no detectable DNase or ATPase activities by itself. These findings are discussed in terms of their implications for regulation of genetic recombination and bacteriophage lambda development.
- Research Organization:
- Univ. of California, Berkeley
- OSTI ID:
- 6744029
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 70:8; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
Similar Records
gamma. protein specified by bacteriophage lambda: structure and inhibitory activity for the recBC enzyme of Escherichia coli
Recombination of bacteriophage phiX174 by the red function of bacteriophage lambda. [Uv radiation]
Genetic and biochemical studies of the lipid-containing bacteriophage PR4
Journal Article
·
Tue Dec 31 23:00:00 EST 1974
· J. Biol. Chem.; (United States)
·
OSTI ID:5143486
Recombination of bacteriophage phiX174 by the red function of bacteriophage lambda. [Uv radiation]
Journal Article
·
Wed Jan 31 23:00:00 EST 1979
· J. Virol.; (United States)
·
OSTI ID:6242554
Genetic and biochemical studies of the lipid-containing bacteriophage PR4
Thesis/Dissertation
·
Sat Dec 31 23:00:00 EST 1988
·
OSTI ID:5525043
Related Subjects
550200* -- Biochemistry
550700 -- Microbiology
59 BASIC BIOLOGICAL SCIENCES
ATP-ASE
BACTERIA
BACTERIOPHAGES
BIOLOGY
CHEMICAL PROPERTIES
DNA-ASE
ENZYMES
ESTERASES
GENE RECOMBINATION
GENES
GENETICS
HYDROLASES
INHIBITION
MICROORGANISMS
MOLECULAR BIOLOGY
MUTANTS
ORGANIC COMPOUNDS
PARASITES
PHOSPHATASES
PROTEINS
PURIFICATION
TEMPERATURE EFFECTS
VIRUSES
550700 -- Microbiology
59 BASIC BIOLOGICAL SCIENCES
ATP-ASE
BACTERIA
BACTERIOPHAGES
BIOLOGY
CHEMICAL PROPERTIES
DNA-ASE
ENZYMES
ESTERASES
GENE RECOMBINATION
GENES
GENETICS
HYDROLASES
INHIBITION
MICROORGANISMS
MOLECULAR BIOLOGY
MUTANTS
ORGANIC COMPOUNDS
PARASITES
PHOSPHATASES
PROTEINS
PURIFICATION
TEMPERATURE EFFECTS
VIRUSES