scholarly journals The release element of the yeast polymerase I transcription terminator can function independently of Reb1p.

1995 ◽  
Vol 15 (11) ◽  
pp. 5929-5936 ◽  
Author(s):  
S W Jeong ◽  
W H Lang ◽  
R H Reeder
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Binding Site ◽  
Mutational Analysis ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Lac Repressor ◽  
Transcription Terminator ◽  
Polymerase I ◽  
Apparent Ability

The Saccharomyces cerevisiae polymerase I (polI) transcription terminator utilizes a DNA-binding protein (Reb1p) as part of a signal that causes the polymerase to pause prior to release from the template. To study the release element of the terminator, independent of the Reb1p pause signal, we have replaced the Reb1p binding site with the binding site for the lac repressor, which acts as a self-contained heterologous pause signal for polI. Release efficiency is maximal when the lac repressor causes polI to pause in exactly the same position that Reb1p would have caused it to pause, suggesting that polI must be precisely positioned for transcript release to occur. Mutational analysis shows that the release element is a region rich in T residues which codes for the extreme 3' end of the transcript and which has no apparent ability to form hairpins when transcribed into RNA. We discuss possible mechanisms whereby this polI release element might function.

scholarly journals Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae.

1992 ◽  
Vol 11 (10) ◽  
pp. 3787-3796 ◽  
Author(s):  
S. Zhang ◽  
C. Lockshin ◽  
A. Herbert ◽  
E. Winter ◽  
A. Rich
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Z Dna

scholarly journals Evi-1, a murine zinc finger proto-oncogene, encodes a sequence-specific DNA-binding protein.

1991 ◽  
Vol 11 (5) ◽  
pp. 2665-2674 ◽  
Author(s):  
A S Perkins ◽  
R Fishel ◽  
N A Jenkins ◽  
N G Copeland
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Zinc Finger ◽  
Sequence Data ◽  
Binding Protein ◽  
Consensus Sequence ◽  
Dna Binding Protein ◽  
Polymerase Chain Reaction Method ◽  
Nucleotide Sequence Data ◽  
Carboxy Terminal

Evi-1 was originally identified as a common site of viral integration in murine myeloid tumors. Evi-1 encodes a 120-kDa polypeptide containing 10 zinc finger motifs located in two domains 380 amino acids apart and an acidic domain located carboxy terminal to the second set of zinc fingers. These features suggest that Evi-1 is a site-specific DNA-binding protein involved in the regulation of RNA transcription. We have purified Evi-1 protein from E. coli and have employed a gel shift-polymerase chain reaction method using random oligonucleotides to identify a high-affinity binding site for Evi-1. The consensus sequence for this binding site is TGACAAGATAA. Evi-1 protein specifically protects this motif from DNase I digestion. By searching the nucleotide sequence data bases, we have found this binding site both in sequences 5' to genes in putative or known regulatory regions and within intron sequences.

scholarly journals COUP-TF (chicken ovalbumin upstream promoter transcription factor)-interacting protein 1 (CTIP1) is a sequence-specific DNA binding protein

2002 ◽  
Vol 368 (2) ◽  
pp. 555-563 ◽  
Author(s):  
Dorina AVRAM ◽  
Andrew FIELDS ◽  
Thanaset SENAWONG ◽  
Acharawan TOPARK-NGARM ◽  
Mark LEID
Keyword(s):  
Transcription Factor ◽  
Immune System ◽  
Dna Binding ◽  
Binding Site ◽  
Binding Protein ◽  
Family Members ◽  
Dna Binding Protein ◽  
Cell Leukaemia ◽  
Upstream Promoter ◽  
Chicken Ovalbumin

Chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting proteins 1 and 2 [CTIP1/Evi9/B cell leukaemia (Bcl) l1a and CTIP2/Bcl11b respectively] are highly related C2H2 zinc finger proteins that are abundantly expressed in brain and the immune system, and are associated with immune system malignancies. A selection procedure was employed to isolate high-affinity DNA binding sites for CTIP1. The core binding site on DNA identified in these studies, 5′-GGCCGG-3′ (upper strand), is highly related to the canonical GC box and was bound by a CTIP1 oligomeric complex(es) in vitro. Furthermore, both CTIP1 and CTIP2 repressed transcription of a reporter gene harbouring a multimerized CTIP binding site, and this repression was neither reversed by trichostatin A (an inhibitor of known class I and II histone deacetylases) nor stimulated by co-transfection of a COUP-TF family member. These results demonstrate that CTIP1 is a sequence-specific DNA binding protein and a bona fide transcriptional repressor that is capable of functioning independently of COUP-TF family members. These findings may be relevant to the physiological and/or pathological action(s) of CTIPs in cells that do not express COUP-TF family members, such as cells of the haematopoietic and immune systems.

scholarly journals A DNA-binding protein is required for termination of transcription by RNA polymerase I in Xenopus laevis.

1990 ◽  
Vol 10 (6) ◽  
pp. 2793-2800 ◽  
Author(s):  
B McStay ◽  
R H Reeder
Keyword(s):  
Dna Binding ◽  
Xenopus Laevis ◽  
Rna Polymerase ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
In Vitro Transcription ◽  
Rna Polymerase I ◽  
Polymerase I ◽  
Terminator Sequence

We describe a partially fractionated in vitro transcription system from Xenopus laevis for the assay of transcription termination by RNA polymerase I. Termination in vitro was found to require a specific terminator sequence in the DNA and a DNA-binding protein fraction that produces a footprint over the terminator sequence.

scholarly journals Novel DNA-binding protein fromDrosophilaembryos identified by binding site selection

FEBS Letters ◽  
1996 ◽  
Vol 396 (1) ◽  
pp. 99-102
Author(s):  
Vesna Todorović ◽  
Snežana Kojić ◽  
Miloš Vujanac ◽  
Ana Savić ◽  
Dragana Stefanović
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Site Selection ◽  
Binding Protein ◽  
Dna Binding Protein
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