hRPB6 is a highly conserved subunit shared by all three RNA polymerases, consisting of 142 amino acid residues. The gene for yeast RPB6 is essential for cell viability and homologues of this subunit exist in archaeal and some viral RNA polymerases. For example the bacterial w (the fifth subunit of the bacterial RNAP core enzyme) and eukaryotic RPB6 are structural homologs. RPB6 has been shown to promote pol II complex assembly, and/or increase its stability, through specific interactions with the largest subunit of RNA pol II. In addition, RPB6 was found to make contact with three small subunits, RPB5, RPB7, and RPB8 and to play a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS.
Forme physique
Clear and colorless frozen liquid solution
Notes préparatoires
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Faites votre choix parmi les versions les plus récentes :
Molecular and cellular biology, 20(4), 1263-1270 (2000-01-29)
The Rpb6 subunit of RNA polymerase II is one of the five subunits common to three forms of eukaryotic RNA polymerase. Deletion and truncation analyses of the rpb6 gene in the fission yeast Schizosaccharomyces pombe indicated that Rpb6, consisting of
Proceedings of the National Academy of Sciences of the United States of America, 98(3), 892-897 (2001-02-07)
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In
RNA polymerases I, II, and III share three subunits that are immunologically and biochemically indistinguishable. The Saccharomyces cerevisiae genes that encode these subunits (RPB5, RPB6, and RPB8) were isolated and sequenced, and their transcriptional start sites were deduced. RPB5 encodes
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