scholarly journals A plant 5S rRNA mimic regulates alternative splicing of transcription factor IIIA pre‐mRNAs

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Ming Chen Hammond ◽  
Andreas Wachter ◽  
Ronald R. Breaker
Keyword(s):  
Transcription Factor ◽  
Alternative Splicing ◽  
5S Rrna ◽  
Transcription Factor Iiia

scholarly journals Displacement of Xenopus transcription factor IIIA from a 5S rRNA gene by a transcribing RNA polymerase.

1991 ◽  
Vol 11 (8) ◽  
pp. 3978-3986 ◽  
Author(s):  
F E Campbell ◽  
D R Setzer
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Internal Control ◽  
Rna Polymerase Iii ◽  
5S Rrna ◽  
Rrna Gene ◽  
Transcription Factor Iiia ◽  
Polymerase Iii ◽  
5S Rrna Gene

In the absence of other components of the RNA polymerase III transcription machinery, transcription factor IIIA (TFIIIA) can be displaced from both strands of its DNA-binding site (the internal control region) on the somatic-type 5S rRNA gene of Xenopus borealis during transcription elongation by bacteriophage T7 RNA polymerase, regardless of which DNA strand is transcribed. Furthermore, substantial displacement is observed after the template has been transcribed only once. Since the complete 5S rRNA transcription complex has previously been shown to remain stably bound to the gene during repeated rounds of transcription by either RNA polymerase III or bacteriophage SP6 RNA polymerase, these results indicate that a factor(s) in addition to TFIIIA is required to create a complex that will remain stably associated with the template during transcription. Thus, transcription complex stability during passage of RNA polymerase cannot be explained solely on the basis of the DNA-binding properties of TFIIIA.

scholarly journals Alternative splicing of anciently exonized 5S rRNA regulates plant transcription factor TFIIIA

2009 ◽  
Vol 19 (5) ◽  
pp. 913-921 ◽  
Author(s):  
Y. Fu ◽  
O. Bannach ◽  
H. Chen ◽  
J.-H. Teune ◽  
A. Schmitz ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Alternative Splicing ◽  
5S Rrna

scholarly journals Maize TF IIIA--the first transcription factor IIIA from monocotyledons. Purification and properties.

1997 ◽  
Vol 44 (3) ◽  
pp. 579-589 ◽  
Author(s):  
E Wyszko ◽  
M Radłowski ◽  
S Bartkowiak ◽  
M Z Barciszewska
Keyword(s):  
Transcription Factor ◽  
Zea Mays L ◽  
Cell Extract ◽  
5S Rrna ◽  
Rrna Gene ◽  
Maize Pollen ◽  
Transcription Factor Iiia ◽  
Purification And Properties ◽  
5S Rrna Gene ◽  
First Time

Purification and properties of transcription factor IIIA (TF IIIA) from maize pollen (Zea mays L.) are presented for the first time. The purified protein has a molecular mass of about 35 kDa and exhibits binding affinity toward both 5S rRNA and 5S rRNA gene. It also facilitates transcription of the 5S rRNA gene in a HeLa cell extract.

Displacement of Xenopus transcription factor IIIA from a 5S rRNA gene by a transcribing RNA polymerase

1991 ◽  
Vol 11 (8) ◽  
pp. 3978-3986
Author(s):  
F E Campbell ◽  
D R Setzer
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Rna Polymerase ◽  
Internal Control ◽  
Rna Polymerase Iii ◽  
5S Rrna ◽  
Rrna Gene ◽  
Transcription Factor Iiia ◽  
Polymerase Iii ◽  
5S Rrna Gene

In the absence of other components of the RNA polymerase III transcription machinery, transcription factor IIIA (TFIIIA) can be displaced from both strands of its DNA-binding site (the internal control region) on the somatic-type 5S rRNA gene of Xenopus borealis during transcription elongation by bacteriophage T7 RNA polymerase, regardless of which DNA strand is transcribed. Furthermore, substantial displacement is observed after the template has been transcribed only once. Since the complete 5S rRNA transcription complex has previously been shown to remain stably bound to the gene during repeated rounds of transcription by either RNA polymerase III or bacteriophage SP6 RNA polymerase, these results indicate that a factor(s) in addition to TFIIIA is required to create a complex that will remain stably associated with the template during transcription. Thus, transcription complex stability during passage of RNA polymerase cannot be explained solely on the basis of the DNA-binding properties of TFIIIA.

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