Transcriptional activator: Difference between revisions
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<StructureSection load='1h89' size='350' side='right' caption='Structure of transcriptional activator C-Myb DNA-binding domain (deeppink) complex with DNA, CAAT/enhancer binding protein β (cyan and green) and K+ ion (purple) (PDB entry [[1h89]])' scene='55/553105/Cv/1'> | <StructureSection load='1h89' size='350' side='right' caption='Structure of transcriptional activator C-Myb DNA-binding domain (deeppink) complex with DNA, CAAT/enhancer binding protein β (cyan and green) and K+ ion (purple) (PDB entry [[1h89]])' scene='55/553105/Cv/1'> | ||
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== Function == | == Function == | ||
'''Transcriptional activators''' (TA) are proteins which bind to DNA and stimulate nearby gene transcription. TA transcription stimulation is achieved by enhancing RNA polymerase binding or by enhancing the formation of open complex which is required for initiation of transcription. TA bind to a specific DNA sequence in or near an operon via their DNA-binding domain (DBD)<ref>PMID:16464826</ref>. | '''Transcriptional activators''' or '''Transcriptional regulators''' (TA) are proteins which bind to DNA and stimulate nearby gene transcription. TA transcription stimulation is achieved by enhancing RNA polymerase binding or by enhancing the formation of open complex which is required for initiation of transcription. TA bind to a specific DNA sequence in or near an operon via their DNA-binding domain (DBD)<ref>PMID:16464826</ref>. '''PrfA''' is an activator of virulence genes in ''Listeria monocytogenes''<ref>PMID:10564496</ref>. See also [[Listeriolysin positive regulatory factor A]]. | ||
== Structural highlights == | == Structural highlights == | ||
TA contains 3 domains: DBD, trans-activating domain (TAD) which binds coregulator proteins and an optional ligand-binding domain (LBD) which senses external signals. | TA contains 3 domains: DBD, trans-activating domain (TAD) which binds coregulator proteins and an optional ligand-binding domain (LBD) which senses external signals. | ||
*<scene name='55/553105/Cv/ | *<scene name='55/553105/Cv/5'>Transcriptional activator C-Myb DNA-binding domain complex with DNA, CAAT/enhancer binding protein β and K+ ion </scene> (PDB entry [[1h89]]). | ||
*<scene name='55/553105/Cv/ | *<scene name='55/553105/Cv/6'>1st K soordination site</scene>. | ||
*<scene name='55/553105/Cv/ | *<scene name='55/553105/Cv/7'>2nd K soordination site</scene>. Water molecules are shown as red spheres. | ||
== 3D Structures of transcriptional activator== | == 3D Structures of transcriptional activator== | ||
[[Transcriptional activator 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Latest revision as of 09:48, 20 August 2024
FunctionTranscriptional activators or Transcriptional regulators (TA) are proteins which bind to DNA and stimulate nearby gene transcription. TA transcription stimulation is achieved by enhancing RNA polymerase binding or by enhancing the formation of open complex which is required for initiation of transcription. TA bind to a specific DNA sequence in or near an operon via their DNA-binding domain (DBD)[1]. PrfA is an activator of virulence genes in Listeria monocytogenes[2]. See also Listeriolysin positive regulatory factor A. Structural highlightsTA contains 3 domains: DBD, trans-activating domain (TAD) which binds coregulator proteins and an optional ligand-binding domain (LBD) which senses external signals.
3D Structures of transcriptional activatorTranscriptional activator 3D structures
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ReferencesReferences
- ↑ Titz B, Thomas S, Rajagopala SV, Chiba T, Ito T, Uetz P. Transcriptional activators in yeast. Nucleic Acids Res. 2006 Feb 7;34(3):955-67. Print 2006. PMID:16464826 doi:http://dx.doi.org/34/3/955
- ↑ Renzoni A, Cossart P, Dramsi S. PrfA, the transcriptional activator of virulence genes, is upregulated during interaction of Listeria monocytogenes with mammalian cells and in eukaryotic cell extracts. Mol Microbiol. 1999 Nov;34(3):552-61. doi: 10.1046/j.1365-2958.1999.01621.x. PMID:10564496 doi:http://dx.doi.org/10.1046/j.1365-2958.1999.01621.x