منابع مشابه
Structural Transitions Mediating Transcription Initiation by T7 RNA Polymerase
During transcription initiation, RNA polymerases appear to retain promoter interactions while transcribing short RNAs that are frequently released from the complex. Upon transition to elongation, the polymerase releases promoter and forms a stable elongation complex. Little is known about the changes in polymerase conformation or polymerase:DNA interactions that occur during this process. To ch...
متن کاملStructural Basis for Substrate Selection by T7 RNA Polymerase
The mechanism by which nucleotide polymerases select the correct substrate is of fundamental importance to the fidelity of DNA replication and transcription. During the nucleotide addition cycle, pol I DNA polymerases undergo the transition from a catalytically inactive "open" to an active "closed" conformation. All known determinants of substrate selection are associated with the "closed" stat...
متن کاملRNA-binding site in T7 RNA polymerase.
Recent models of RNA polymerase transcription complexes have invoked the idea that enzyme-nascent RNA contacts contribute to the stability of the complexes. Although much progress on this topic has been made with the multisubunit Escherichia coli RNA polymerase, there is a paucity of information regarding the structure of single-subunit phage RNA polymerase transcription complexes. Here, we pho...
متن کاملInhibition of T7 RNA polymerase by T7 lysozyme in vitro.
The in vivo observation that the expression of bacteriophage T7 gene 3.5 (T7 lysozyme) inactivates T7 class II transcription and the in vitro observation that T7 lysozyme inhibits T7 RNA polymerase lead to the hypothesis that T7 lysozyme might preferentially inhibit transcription from T7 class II promoters. T7 lysozyme was cloned into a lambda pL expression vector, overproduced in Escherichia c...
متن کاملPromoter specificity determinants of T7 RNA polymerase.
The high specificity of T7 RNA polymerase (RNAP) for its promoter sequence is mediated, in part, by a specificity loop (residues 742-773) that projects into the DNA binding cleft (1). Previous work demonstrated a role for the amino acid residue at position 748 (N748) in this loop in discrimination of the base pairs (bp) at positions -10 and -11 (2). A comparison of the sequences of other phage ...
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ژورنال
عنوان ژورنال: Uirusu
سال: 2001
ISSN: 0042-6857,1884-3433
DOI: 10.2222/jsv.51.81