Purification and properties of a λ operator-binding protein which is expected to be autorepressor (tof protein) from E. coli carrying ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1977-01

AUTHORS

Tomoaki Murotsu, Hiroshi Tanaka, Masami Imaji, Hideo Koga, Kenichi Matsubara, Tadao Horiuchi

ABSTRACT

In order to study the mode of action of the tof gene product, which is an “autorepressor” of the bacteriophage λ and plasmid λdv, we have purified a DNA-binding protein which is specifically produced in bacteria carrying λdv. This protein possesses characteristics expected for the product of the tof gene, since it is produced under conditions where cI-repressor is not made, and since it binds to oL and oR operators on the λ phage genome. The molecular weight of the native protein is 16,000–17,000 daltons, and the monomeric molecular weight as measured by gel electrophoresis in the presence of sodium dodecyl sulfate is about 10,000 daltons. Denaturation and renaturation experiments demonstrated that the native protein is a dimer of 10,000-dalton monomers. The λDNA-specific binding protein is not produced in cells carrying i21dv or Φ80dv. More... »

PAGES

139-147

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00267391

DOI

http://dx.doi.org/10.1007/bf00267391

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009590784

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/340920


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