hRPB3 (p33) is a highly conserved subunit shared by all three RNA polymerases. It has been shown to be in close contact to promoter DNA when pol II is recruited into the preinitiation complex. RPB3 has also been implicated in direct protein-protein contacts with transcription factor IIB, Rap30 subunit of transcription factor IIF, and gene-specific modulator proteins, such as the hepatitis B virus transactivator protein X or an inhibitor of pol II, RMP (RPB3-mediating protein). Therefore, RPB3 is facilitating the communication between the pol II core and a variety of basal and gene-specific transcription factors. In the pol II complex, RPB3 interacts with RPB5 and the RPB3–RPB5 interaction is intensified in the presence of three subunits, RPB7, RPB8 and RPB11. RPB3 also makes direct contacts with both RPB1 and RPB2, the two large subunits of the polymerase complex.
forma física
Clear and colorless frozen liquid solution
Nota de preparo
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Proceedings of the National Academy of Sciences of the United States of America, 94(23), 12268-12273 (1997-11-14)
By using site-specific protein-DNA photocrosslinking, we define the positions of TATA-binding protein, transcription factor IIB, transcription factor IIF, and subunits of RNA polymerase II (RNAPII) relative to promoter DNA within the human transcription preinitiation complex. The results indicate that the
The Journal of biological chemistry, 272(11), 7132-7139 (1997-03-14)
Hepatitis B virus X protein (HBx) transactivates viral and cellular genes through a wide variety of cis-elements. However, the mechanism is still obscure. Our finding that HBx directly interacts with RNA polymerase II subunit 5 (RPB5), a common subunit of
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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