منابع مشابه
Evidence for DNA bending at the T7 RNA polymerase promoter.
Phage T7 RNA polymerase is the only DNA-dependent RNA polymerase for which we have a high-resolution structure of the promoter-bound complex. Recent studies with the more complex RNA polymerases have suggested a role for DNA wrapping in the initiation of transcription. Here, circular permutation gel retardation assays provide evidence that the polymerase does indeed bend its promoter DNA. A com...
متن کاملDNA sequence analysis with a modified bacteriophage T7 DNA polymerase.
A chemically modified phage T7 DNA polymerase has three properties that make it ideal for DNA sequencing by the chain-termination method. The enzyme is highly processive, catalyzing the polymerization of thousands of nucleotides without dissociating. By virtue of the modification the 3' to 5' exonuclease activity is eliminated. The modified polymerase efficiently uses nucleotide analogs that in...
متن کاملNucleotide sequence of an RNA polymerase binding site at an early T7 promoter.
Escherichia coli RNA polymerase (EC 2.7.7.6), bound in a tight complex at an early T7 promoter, protects 41 to 43 base pairs of DNA from digestion by DNase. I. The protected DNA fragment contains both the binding site for RNA polymerase and the mRNA initiation point for the promoter. The sequence of the DNA fragment and the sequence of the mRNA that it codes for are presented here. A seven-base...
متن کاملSignal integration at the c-fos promoter.
The c-fos gene encodes a basic region-leucine zipper transcription factor that requires heterodimerization with a member of the Jun family for stable DNA binding. Fos/Jun heterodimers are present in the AP-1 transcription factor complex and both c-Fos and c-Jun are capable of transforming cells (1). Continuous expression of c-fos can lead to aberrant differentiation (2) but may also sometimes b...
متن کاملC-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA.
Single-stranded DNA-binding protein (gp2.5), encoded by gene 2.5 of bacteriophage T7, plays an essential role in DNA replication. Not only does it remove impediments of secondary structure in the DNA, it also modulates the activities of the other replication proteins. The acidic C-terminal tail of gp2.5, bearing a C-terminal phenylalanine, physically and functionally interacts with the helicase...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1979
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/6.2.525