A computerized method for mapping RNA polymerase binding sites on adenovirus 2 DNA.
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to S Surzycki.
Explore the source record for details and available documents.
Antisera prepared against purified Chlamydomonas reinhardi small chloroplast ribosomal subunit, judged homogenous by sucrose gradient velocity sedimentation and RNA gel electrophoresis was immunologically cross reactive with E. coli ribosomal proteins. The results of three different experimental approaches, namely Ouchterlony double diffusion, sucrose gradient velocity sedimentation and two dimensional crossed immunoelectrophoresis indicate that both E. coli ribosomal subunits and the chloroplast large ribosomal subunit contain proteins which show antigenic similarity to the chloroplast small ribosomal subunit proteins. However, cytoplasmic ribosomal subunits did not contain proteins which were cross reactive with immune antisera.
Polyriboinosinic acid (poly I) inhibits initiation of transcription by binary complexes formed between Adenovirus 2 DNA and E. coli RNA polymerase holoenzyme. In the presence of poly I, just as in the presence of rifampicin, initiation of transcription exhibits a sigmoidal dependence on the temperature at which the binary complexes are formed. This indicates that I (closed) complexes between Ad 2 DNA and RNA polymerase are rapidly inactivated by poly I, but that RS (open) complexes are relatively resistant. However, even among the RS complexes, at least two classes can be distinguished on the basis of the degree to which they are resistant to poly I: RS-1 complexes are somewhat sensitive to poly I (half-time of inactivation approximately 10 min) while RS-2 complexes are almost completely resistant to the inhibitor (half-time of inactivation approximately 10 h). For both types of RS complex, the degree of sensitivity to poly I is ionic strength-dependent.
Explore the source record for details and available documents.
Explore the source record for details and available documents.