Structural plasticity of T4 transcription co-activator gp33 revealed by a protease-resistant unfolded state
Author:
Funder
Department of Biotechnology, Govt. of India
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Transcription of the T4 late genes;Geiduschek;Virol. J.,2010
2. Mutational and functional analysis of a segment of the sigma family bacteriophage T4 late promoter recognition protein gp55;Wong;J. Biol. Chem.,2003
3. The mechanism of transcriptional activation by the topologically DNA-linked sliding clamp of bacteriophage T4;Kolesky;J. Mol. Biol.,2002
4. Transcriptional activation by a DNA-tracking protein: structural consequences of enhancement at the T4 late promoter;Tinker;Cell,1994
5. Crystal structure of the bacteriophage T4 late-transcription coactivator gp33 with the β-subunit flap domain of Escherichia coli RNA polymerase;Twist;Proc. Natl. Acad. Sci. U. S. A.,2011
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