The role of the central zinc fingers of transcription factor IIIA in binding to 5 S RNA 1 1Edited by D. E. Draper

2000 ◽  
Vol 301 (1) ◽  
pp. 47-60 ◽  
Author(s):  
M.A Searles ◽  
D Lu ◽  
A Klug
Keyword(s):  
Transcription Factor ◽  
Zinc Fingers ◽  
Transcription Factor Iiia

Transcription factor IIIA (TFIIIA) in the second decade

1996 ◽  
Vol 109 (3) ◽  
pp. 535-539 ◽  
Author(s):  
B.S. Shastry
Keyword(s):  
Transcription Factor ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Rna Binding ◽  
Current Knowledge ◽  
Zinc Fingers ◽  
Specific Factor ◽  
Transcription Factor Iiia ◽  
Dna And Rna

Transcription factor IIIA is a very extensively studied eukaryotic gene specific factor. It is a special member of the zinc finger family of nucleic acid binding proteins with multiple functions. Its N-terminal polypeptide (280 amino acid residue containing peptide; finger containing region) carries out sequence specific DNA and RNA binding and the C-terminal peptide (65 amino acid residue containing peptide; non-finger region) is involved in the transactivation process possibly by interacting with other general factors. It is a unique factor in the sense that it binds to two structurally different nucleic acids, DNA and RNA. It accomplishes this function through its zinc fingers, which are arranged into a cluster of nine motifs. Over the past three years there has been considerable interest in determining the structural features of zinc fingers, identifying the fingers that preferentially recognize DNA and RNA, defining the role of metal binding ligands and the linker region in promotor recognition and the role of C-terminal amino acid sequence in the gene activation. This article briefly reviews our current knowledge on this special protein in these areas.

Relative Contributions of the Zinc Fingers of Transcription Factor IIIA to the Energetics of DNA Binding

1994 ◽  
Vol 244 (1) ◽  
pp. 23-25 ◽  
Author(s):  
Karen R. Clemens ◽  
Penghua Zhang ◽  
Xiubei Liao ◽  
Steven J. McBryant ◽  
Peter E. Wright ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Zinc Fingers ◽  
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.

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.

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
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