The role of highly conserved single-stranded nucleotides of Xenopus 5S RNA in the binding of transcription factor IIIA

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1388-1395 ◽  
Author(s):  
Paul J. Romaniuk
Keyword(s):  
Transcription Factor ◽  
5S Rna ◽  
Transcription Factor Iiia

Proteolytic footprinting of transcription factor TFIIIA reveals different tightly binding sites for 5S RNA and 5S DNA

1993 ◽  
Vol 13 (9) ◽  
pp. 5149-5158
Author(s):  
D F Bogenhagen
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Zinc Fingers ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
5S Rna ◽  
Transcription Factor Iiia ◽  
Tryptic Fragment ◽  
N Terminus ◽  
5S Dna

Transcription factor IIIA (TFIIIA) employs an array of nine N-terminal zinc fingers to bind specifically to both 5S RNA and 5S DNA. The binding of TFIIIA to 5S RNA and 5S DNA was studied by using a protease footprinting technique. Brief treatment of free or bound TFIIA with trypsin or chymotrypsin generated fragments which were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Fragments retaining the N terminus of TFIIA were identified by immunoblotting with an antibody directed against the N terminus of TFIIIA. Proteolytic footprinting of TFIIIA complexed with 5S DNA derivatives reinforced other evidence that the three N-terminal zinc fingers of TFIIIA bind most tightly to 5S DNA. Proteolytic footprinting of TFIIIA in reconstituted 7S ribonucleoprotein particles revealed different patterns of trypsin sensitivity for TFIIIA bound to oocyte versus somatic 5S RNA. Trypsin cleaved TFIIIA between zinc fingers 3 and 4 more readily when the protein was bound to somatic 5S RNA than when it was bound to oocyte 5S RNA. A tryptic fragment of TFIIIA containing zinc fingers 4 through 7 remained tightly associated with somatic 5S RNA. Zinc fingers 4 through 7 may represent a tightly binding site for 5S RNA in the same sense that fingers 1 through 3 represent a tightly binding site for 5S DNA.

The C-terminal domain of transcription factor IIIA interacts differently with different 5S RNA genes

1989 ◽  
Vol 9 (2) ◽  
pp. 499-514
Author(s):  
Y Y Xing ◽  
A Worcel
Keyword(s):  
Transcription Factor ◽  
Site Directed Mutagenesis ◽  
5S Rna ◽  
Transcription Factor Iiia ◽  
5S Dna ◽  
Type Site ◽  
Single Trace ◽  
Dna Complex ◽  
5S Rna Genes ◽  
Rna Genes

DNase I footprints and affinity measurements showed that the C-terminal arm of Xenopus transcription factor IIIA interacts differently with different Xenopus 5S DNAs, forming three distinct types of transcription factor IIIA-5S DNA complexes: a somatic type, a major-oocyte (and pseudogene) type, and a trace-oocyte type. Site-directed mutagenesis on the major-oocyte 5S gene revealed that somatic-type changes at positions 53, 55, and 56 changed the structure of the transcription factor IIIA-5S DNA complex from major-oocyte to somatic, and a single trace-oocyte change at position 56 caused the change from major-oocyte to trace-oocyte complex. We further show that the somatic-type changes are accompanied by a marked enhancement in the rate of 5S RNA transcription, and we discuss the possible biological relevance of these findings.

scholarly journals Proteolytic footprinting of transcription factor TFIIIA reveals different tightly binding sites for 5S RNA and 5S DNA.

1993 ◽  
Vol 13 (9) ◽  
pp. 5149-5158 ◽  
Author(s):  
D F Bogenhagen
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Zinc Fingers ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
5S Rna ◽  
Transcription Factor Iiia ◽  
Tryptic Fragment ◽  
N Terminus ◽  
5S Dna

Transcription factor IIIA (TFIIIA) employs an array of nine N-terminal zinc fingers to bind specifically to both 5S RNA and 5S DNA. The binding of TFIIIA to 5S RNA and 5S DNA was studied by using a protease footprinting technique. Brief treatment of free or bound TFIIA with trypsin or chymotrypsin generated fragments which were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Fragments retaining the N terminus of TFIIA were identified by immunoblotting with an antibody directed against the N terminus of TFIIIA. Proteolytic footprinting of TFIIIA complexed with 5S DNA derivatives reinforced other evidence that the three N-terminal zinc fingers of TFIIIA bind most tightly to 5S DNA. Proteolytic footprinting of TFIIIA in reconstituted 7S ribonucleoprotein particles revealed different patterns of trypsin sensitivity for TFIIIA bound to oocyte versus somatic 5S RNA. Trypsin cleaved TFIIIA between zinc fingers 3 and 4 more readily when the protein was bound to somatic 5S RNA than when it was bound to oocyte 5S RNA. A tryptic fragment of TFIIIA containing zinc fingers 4 through 7 remained tightly associated with somatic 5S RNA. Zinc fingers 4 through 7 may represent a tightly binding site for 5S RNA in the same sense that fingers 1 through 3 represent a tightly binding site for 5S DNA.

scholarly journals Restoration of binding of oxidized transcription factor IIIA to 5S RNA by thioredoxin

1988 ◽  
Vol 16 (17) ◽  
pp. 8497-8507 ◽  
Author(s):  
Ricardo L. Pastori ◽  
Keith E. Zucker ◽  
Yan Yan Xing
Keyword(s):  
Transcription Factor ◽  
5S Rna ◽  
Transcription Factor Iiia

scholarly journals The C-terminal domain of transcription factor IIIA interacts differently with different 5S RNA genes.

1989 ◽  
Vol 9 (2) ◽  
pp. 499-514 ◽  
Author(s):  
Y Y Xing ◽  
A Worcel
Keyword(s):  
Transcription Factor ◽  
Site Directed Mutagenesis ◽  
5S Rna ◽  
Transcription Factor Iiia ◽  
5S Dna ◽  
Type Site ◽  
Single Trace ◽  
Dna Complex ◽  
5S Rna Genes ◽  
Rna Genes

DNase I footprints and affinity measurements showed that the C-terminal arm of Xenopus transcription factor IIIA interacts differently with different Xenopus 5S DNAs, forming three distinct types of transcription factor IIIA-5S DNA complexes: a somatic type, a major-oocyte (and pseudogene) type, and a trace-oocyte type. Site-directed mutagenesis on the major-oocyte 5S gene revealed that somatic-type changes at positions 53, 55, and 56 changed the structure of the transcription factor IIIA-5S DNA complex from major-oocyte to somatic, and a single trace-oocyte change at position 56 caused the change from major-oocyte to trace-oocyte complex. We further show that the somatic-type changes are accompanied by a marked enhancement in the rate of 5S RNA transcription, and we discuss the possible biological relevance of these findings.

Induced Fit and “Lock and Key” Recognition of 5S RNA by Zinc Fingers of Transcription Factor IIIA

2006 ◽  
Vol 357 (1) ◽  
pp. 275-291 ◽  
Author(s):  
Brian M. Lee ◽  
Jing Xu ◽  
Bryan K. Clarkson ◽  
Maria A. Martinez-Yamout ◽  
H. Jane Dyson ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Zinc Fingers ◽  
5S Rna ◽  
Induced Fit ◽  
Transcription Factor Iiia

Mutations in 5S DNA and 5S RNA have different effects on the binding of Xenopus transcription factor IIIA

Biochemistry ◽  
1991 ◽  
Vol 30 (9) ◽  
pp. 2495-2500 ◽  
Author(s):  
Qimin You ◽  
Nik Veldhoen ◽  
Florence Baudin ◽  
Paul J. Romaniuk
Keyword(s):  
Transcription Factor ◽  
5S Rna ◽  
Transcription Factor Iiia ◽  
5S Dna
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