TFIID: Difference between revisions

From The School of Biomedical Sciences Wiki
Jump to navigation Jump to search
Created page with "'''TFIID''' (also known as '''transcription factor II D''') is a multi-subunit general transcription factor involved in the formation of the pre-initiation complex (Hartl, 2009, ..."
 
Nnjm2 (talk | contribs)
7,735 edits
removed some unnecessary html.
 
(8 intermediate revisions by 5 users not shown)
Line 1: Line 1:
'''TFIID''' (also known as '''transcription factor II D''') is a multi-subunit general transcription factor involved in the formation of the pre-initiation complex (Hartl, 2009, p.406) TFIID binding is involved in the first step of transcription in eukaryotes. It later goes on to associate with RNA polymerase II , which is used to transcribe mRNA.
TFIID (also known as [[Transcription factor|transcription factor]] II D) is a multi-subunit general transcription factor involved in the formation of the pre-initiation complex<ref>Hartl, D.L., Jones, E.W., 2009. Genetics; Analysis of Genes and Genomes. 7th ed. Jones and Bartlett Publications.</ref>. TFIID binding is involved in the first step of transcription in [[Eukaryotes|eukaryotes]]. It later goes on to associate with [[RNA polymerase II|RNA polymerase II]], which is used to transcribe [[RNA polymerase II|mRNA]].  


= Structure =
== Structure ==


TFIID is comprised of a TATA-binding protein (TBP) and a complex of 10 TBP-associated factors (TAFs). The TBP&nbsp;region is required by all three RNA polymerases, whereas the TAF regions differ by RNA&nbsp;polymerase (Gupta, 2007, p.537). TBP is composed of 180 amino acid residues and is highly conserved throughout evolution (White, 2001, p.45).
Using [[Electron microscopy|electron microscopy]] to study both human and [[Yeast|yeast]] TFIID's had led scientists to discover that both have a trilobular structure. TFIID is comprised of a [[TATA-binding protein|TATA-binding protein]] (TBP) and a complex of 10 [[TBP-associated factors|TBP-associated factors]] (TAFs). The TBP region is required by all three [[RNA polymerase II|RNA polymerases]], whereas the TAF regions differ by RNA polymerase<ref>Gupta, P.K., 2007. Genetics; Classical to Modern. 1st ed. Rastogi Publications</ref>. TBP is composed of 180 [[Amino acids|amino acid]] residues and is highly conserved throughout evolution<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>.  


= Mechanism =
== Mechanism ==


TBP recognises and binds to the TATA box in eukaryotic genes as&nbsp;per it's main function&nbsp;(Hartl, 2009, p.406). The TAF subunits are not required in genes with a TATA promoter, however they do have a role in reducing transcription levels by dissociating TBP from the TATA&nbsp;box (White, 2001, p.54).
TBP recognises and binds to the [[TATA box|TATA box]] in eukaryotic genes as per it's main function<ref>Hartl, D.L., Jones, E.W., 2009. Genetics; Analysis of Genes and Genomes. 7th ed. Jones and Bartlett Publications.</ref>. The TAF subunits are not required in genes with a [[TATA promoter|TATA promoter]]. However, they do have a role in reducing transcription levels by dissociating TBP from the TATA box<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>.  


Unlike other proteins with DNA binding domains, TBP notably alters the structure of DNA when bound via twisting and bending it (White, 2001, p.47). This creates a hydrophobic exposed region for TFIIB to join to in the next step of pre-initiation complex formation (White, 2001, p.55).
Unlike other [[Proteins|proteins]] with [[DNA binding domains|DNA binding domains]], TBP notably alters the structure of [[DNA|DNA]] when bound via twisting and bending it<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>. This creates a [[Hydrophobic|hydrophobic]] exposed region for TFIIB to join to in the next step of pre-initiation complex formation<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>.  


= Function =
== Function ==


While the main function of the TBP region of TFIID is to bind to the TATA&nbsp;box on DNA, the TAF&nbsp;proteins have a range of functions. Notably, TAFII250 acts as a scaffold protein and has kinase activity, and TAFII150 binds to DNA downstream of the TATA box (White, 2001, p.54). Furthermore, TAFII80, TAFII31 and TAFII20 have show similar features and structures to histones H4, H3 and H2b respectibly (White, 2001, p.54).  
While the main function of the TBP region of TFIID is to bind to the TATA box on DNA, the TAF proteins have a range of functions. Notably, TAFII250 acts as a [[Scaffold protein|scaffold protein]] and has [[Kinase|kinase]] activity, and TAFII150 binds to DNA downstream of the TATA box<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>. Furthermore, TAFII80, TAFII31 and TAFII20 have shown similar features and structures to histones H4, H3 and H2b respectively<ref>White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.</ref>.  


&nbsp;
== References  ==


<references />
<references />
Gupta, P.K., 2007. ''Genetics; Classical to Modern. ''1st ed. Rastogi Publications.
Hartl, D.L., Jones, E.W., 2009. ''Genetics; Analysis of Genes and Genomes''. 7th ed. Jones and Bartlett Publications.
White, R.J., 2001. ''Gene Transcription; Mechanisms and Control''. 1st ed. Blackwell Science Ltd.

Latest revision as of 14:46, 1 November 2018

TFIID (also known as transcription factor II D) is a multi-subunit general transcription factor involved in the formation of the pre-initiation complex[1]. TFIID binding is involved in the first step of transcription in eukaryotes. It later goes on to associate with RNA polymerase II, which is used to transcribe mRNA.

Structure

Using electron microscopy to study both human and yeast TFIID's had led scientists to discover that both have a trilobular structure. TFIID is comprised of a TATA-binding protein (TBP) and a complex of 10 TBP-associated factors (TAFs). The TBP region is required by all three RNA polymerases, whereas the TAF regions differ by RNA polymerase[2]. TBP is composed of 180 amino acid residues and is highly conserved throughout evolution[3].

Mechanism

TBP recognises and binds to the TATA box in eukaryotic genes as per it's main function[4]. The TAF subunits are not required in genes with a TATA promoter. However, they do have a role in reducing transcription levels by dissociating TBP from the TATA box[5].

Unlike other proteins with DNA binding domains, TBP notably alters the structure of DNA when bound via twisting and bending it[6]. This creates a hydrophobic exposed region for TFIIB to join to in the next step of pre-initiation complex formation[7].

Function

While the main function of the TBP region of TFIID is to bind to the TATA box on DNA, the TAF proteins have a range of functions. Notably, TAFII250 acts as a scaffold protein and has kinase activity, and TAFII150 binds to DNA downstream of the TATA box[8]. Furthermore, TAFII80, TAFII31 and TAFII20 have shown similar features and structures to histones H4, H3 and H2b respectively[9].

References

  1. ↑ Hartl, D.L., Jones, E.W., 2009. Genetics; Analysis of Genes and Genomes. 7th ed. Jones and Bartlett Publications.
  2. ↑ Gupta, P.K., 2007. Genetics; Classical to Modern. 1st ed. Rastogi Publications
  3. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
  4. ↑ Hartl, D.L., Jones, E.W., 2009. Genetics; Analysis of Genes and Genomes. 7th ed. Jones and Bartlett Publications.
  5. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
  6. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
  7. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
  8. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
  9. ↑ White, R.J., 2001. Gene Transcription; Mechanisms and Control. 1st ed. Blackwell Science Ltd.
Retrieved from "https://teaching.ncl.ac.uk/bms/wiki//index.php?title=TFIID&oldid=21835"