EUKARYOTIC RNA POLYMERASE TRANSCRIPTION FACTORS Rather than just a sigma factor to recognize the promoter in conjunction with the pol recognized by a multi-subunit complex called transcription factor (TBP) and several TBP-associated factors (TAFS) wherein binding occurs independent transcription factors are needed. TF attaches to the TFIID while stabilizing the complex. TFIIF attaches to TFIID and TFIIB to allow docking of the RNA begin transcription: two more factors are required. TF binds TFII attaches to RNA Polymerase lI, providing a helicase activity need allow the polymerase to read one of them. TF also has another c phosphorylates RŅA polymerase Il's carboxyl-terminal domain (CTD). The CTD conta successively phosphorylated, forma (negatively charged) tail that aids in the separatic

Human Anatomy & Physiology (11th Edition)
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EUKARYOTIC RNA POLYMERASE TRANSCRIPTION FACTORS
Rather than just a sigma factor to recognize the promoter in conjunction with the polymerase core enzyme, the eukaryotic promoter is
recognized by a multi-subunit complex called transcription factor
which is comprised of TATA-binding protein
(TBP) and several TBP-associated factors (TAFS) wherein binding occurs independently of RNA Polymerase II. After this, two
transcription factors are needed. TF
attaches to the TFI|D while TF
to the nearby DNA,
stabilizing the complex. TFIIF attaches to TFIID and TFIIB to allow docking of the RNA Polymerase
The complex is still not ready to
begin transcription: two more factors are required. TF
binds TFIIF and RNA Polymerase II, and finally, TF
attaches to RNA Polymerase II, providing a helicase activity needed to pry apart the two strands of DNA and
allow the polymerase to read one of them. TF
also has another crucial enzymatic function: it is a serine kinase that
phosphorylates RŅA polymerase Il's carboxyl-terminal domain (CTD). The CTD contains numerous serines that, as they are
successively phosphorylated, form a (negatively charged) tail that aids in the separation of the RNẠP II and the TFIID/promoter.
Transcribed Image Text:EUKARYOTIC RNA POLYMERASE TRANSCRIPTION FACTORS Rather than just a sigma factor to recognize the promoter in conjunction with the polymerase core enzyme, the eukaryotic promoter is recognized by a multi-subunit complex called transcription factor which is comprised of TATA-binding protein (TBP) and several TBP-associated factors (TAFS) wherein binding occurs independently of RNA Polymerase II. After this, two transcription factors are needed. TF attaches to the TFI|D while TF to the nearby DNA, stabilizing the complex. TFIIF attaches to TFIID and TFIIB to allow docking of the RNA Polymerase The complex is still not ready to begin transcription: two more factors are required. TF binds TFIIF and RNA Polymerase II, and finally, TF attaches to RNA Polymerase II, providing a helicase activity needed to pry apart the two strands of DNA and allow the polymerase to read one of them. TF also has another crucial enzymatic function: it is a serine kinase that phosphorylates RŅA polymerase Il's carboxyl-terminal domain (CTD). The CTD contains numerous serines that, as they are successively phosphorylated, form a (negatively charged) tail that aids in the separation of the RNẠP II and the TFIID/promoter.
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