RNA polymerase structure-function: insights into points of transcriptional regulation.
The crystal structure of Thermus aquaticus RNA polymerase (RNAP) with 3.3 A resolution has recently been described. The high degree of sequence similarity between T. aquaticus RNAP and the prototypical RNAP from Escherichia coli invites comparison of the new structural data with genetic and biochemical results that defined the interaction sites of E. coli RNAP with transcription regulators.
Severinov
K
K
Department of Genetics, Rutgers, Waksman Institute, The State University of New Jersey, Piscataway, NJ 08854, USA. severik@waksman. rutgers.edu
D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D015964:Gene Expression Regulation, Bacterial; D008958:Models, Molecular; D013824:Thermus / Q000201:enzymology*; D014157:Transcription Factors / Q000378:metabolism; D014158:Transcription, Genetic / Q000235:genetics*
D014157:Transcription Factors; D012321:DNA-Directed RNA Polymerases