Asymmetric transcription of R plasmid NR1 in Proteus mirabilis.
AUTOR(ES)
Appelbaum, E R
RESUMO
The composite R plasmid NR1, its resistance transfer factor which specifies resistance to tetracycline (RTF-Tc component), and its r-determinants component were each denatured and centrifuged to equilibrium in CsCl density gradients containing polyuridylic acid-polyguanidylic acid. The complementary deoxyribonucleic acid strands of NR1 and the complementary strands of the RTF-Tc component could be separated by this technique because of a threefold difference in polyuridylic acid-polyguanidylic acid binding to the strands of the RTF-Tc component. The two strands of the r-determinants component bound equal amounts of polyuridylic acid-polyguanidylic acid. Hybridization of single strands of plasmid deoxyribonucleic acid with in vivo-labeled ribonucleic acid from Proteus mirabilis containing NR1 indicated that transcription within the RTF-Tc component is from the NR1 strand which preferentially binds polyuridylic acid-polyguanidylic acid, whereas transcription within the r-determinants component is predominantly from the complementary strand.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=218117Documentos Relacionados
- Transition of R factor NR1 in Proteus mirabilis: molecular structure and replication of NR1 deoxyribonucleic acid.
- Transition of the R factor NR1 and Proteus mirabilis: level of drug resistance of nontransitioned and transitioned cells.
- Transposon mutagenesis in Proteus mirabilis.
- Lipoprotein from Proteus mirabilis.
- Structure, function, and regulation of Escherichia coli rRNA in Proteus mirabilis.
