Digitale Medien
Springer
Molecular genetics and genomics
118 (1972), S. 199-207
ISSN:
1617-4623
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Summary Although a large number of E. coli RNA polymerase molecules can bind to phage T3 DNA, not more than three remain bound per DNA template after addition of poly inosinic acid (poly I) which has a high affinity for the enzyme. These stable complexes are able to initiate RNA chains without lag as the enzyme is resistant against rifampicin if substrate is added simultaneously with the drug. Poly I resistant complexes decay very rapidly in the cold (Fig. 2) and are not formed in the absence of the polymerase σ factor (Table 2). The data provide additional support for the idea that the σ factor effects the binding of the enzymes to specific sites on the DNA template.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00333456
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