Publications
2000
Schaub M, Krol A, Carbon P
Structural organization of Staf-DNA complexes Article de journal
Dans: Nucleic Acids Res, vol. 28, no. 10, p. 2114-2121, 2000, ISBN: 10773080, (1362-4962 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Animals Base Sequence Binding Sites DNA-Binding Proteins/*chemistry/*metabolism Human Models, Amino Acid-Specific/*genetics Support, Genetic Trans-Activators/*chemistry/*metabolism Vertebrates Xenopus laevis Zinc Fingers, Molecular Molecular Sequence Data Nucleic Acid Conformation Plasmids/*chemistry/*metabolism Protein Conformation RNA, Non-U.S. Gov't Templates, Small Nuclear/*genetics RNA, Transfer, Unité ARN
@article{,
title = {Structural organization of Staf-DNA complexes},
author = {M Schaub and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10773080},
isbn = {10773080},
year = {2000},
date = {2000-01-01},
journal = {Nucleic Acids Res},
volume = {28},
number = {10},
pages = {2114-2121},
abstract = {The transactivator Staf, which contains seven contiguous zinc fingers of the C(2)-H(2)type, exerts its effects on gene expression by binding to specific targets in vertebrate small nuclear RNA (snRNA) and snRNA-type gene promoters. Here, we have investigated the interaction of the Staf zinc finger domain with the optimal Xenopus selenocysteine tRNA (xtRNA(Sec)) and human U6 snRNA (hU6) Staf motifs. Generation of a series of polypeptides containing increasing numbers of Staf zinc fingers tested in binding assays, by interference techniques and by binding site selection served to elucidate the mode of interaction between the zinc fingers and the Staf motifs. Our results provide strong evidence that zinc fingers 3-6 represent the minimal zinc finger region for high affinity binding to Staf motifs. Furthermore, we show that the binding of Staf is achieved through a broad spectrum of close contacts between zinc fingers 1-6 and xtRNA(Sec)or optimal sites or between zinc fingers 3-6 and the hU6 site. Extensive DNA major groove contacts contribute to the interaction with Staf that associates more closely with the non-template than with the template strand. Based on these findings and the structural information provided by the solved structures of other zinc finger-DNA complexes, we propose a model for the interaction between Staf zinc fingers and the xtRNA(Sec), optimal and hU6 sites.},
note = {1362-4962
Journal Article},
keywords = {Amino Acid Sequence Animals Base Sequence Binding Sites DNA-Binding Proteins/*chemistry/*metabolism Human Models, Amino Acid-Specific/*genetics Support, Genetic Trans-Activators/*chemistry/*metabolism Vertebrates Xenopus laevis Zinc Fingers, Molecular Molecular Sequence Data Nucleic Acid Conformation Plasmids/*chemistry/*metabolism Protein Conformation RNA, Non-U.S. Gov't Templates, Small Nuclear/*genetics RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1999
Schaub M, Krol A, Carbon P
Flexible zinc finger requirement for binding of the transcriptional activator staf to U6 small nuclear RNA and tRNA(Sec) promoters Article de journal
Dans: J Biol Chem, vol. 274, no. 34, p. 24241-24249, 1999, ISBN: 10446199, (0021-9258 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence Animals Binding Sites DNA-Binding Proteins/chemistry/*metabolism Deoxyribonuclease I/pharmacology Human Molecular Sequence Data *Promoter Regions (Genetics) RNA, Amino Acid-Specific/*genetics Support, Non-U.S. Gov't Trans-Activators/chemistry/*metabolism Xenopus *Zinc Fingers, Small Nuclear/*genetics RNA, Transfer, Unité ARN
@article{,
title = {Flexible zinc finger requirement for binding of the transcriptional activator staf to U6 small nuclear RNA and tRNA(Sec) promoters},
author = {M Schaub and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10446199},
isbn = {10446199},
year = {1999},
date = {1999-01-01},
journal = {J Biol Chem},
volume = {274},
number = {34},
pages = {24241-24249},
abstract = {The transactivator Staf, which contains seven zinc finger motifs, exerts its effect on gene expression by binding to specific targets in small nuclear RNA (snRNA) and snRNA-type gene promoters. In this work, binding site selection allowed us to identify the 21-base pair ATTACCCATAATGCATYGCGG sequence as the high affinity consensus binding site for Staf. It shows a high sequence divergence with Staf-responsive elements in the Xenopus selenocysteine tRNA (tRNA(Sec)) and human U6 snRNA promoters. By using a combination of approaches, we analyzed the interaction of wild-type and truncated Staf zinc finger domains with the consensus, Xenopus tRNA(Sec), and human U6 sites. Two main conclusions emerged from our data. First, the data clearly indicate that zinc finger 7 does not establish base-specific contacts in Staf-DNA complexes. The second conclusion concerns zinc finger 1, which is required for the binding to the Xenopus tRNA(Sec) site but is dispensable in the case of the human U6 site. Taking into account the sequence differences in the two sites, these findings demonstrate that Staf utilizes zinc finger 1 in a rather flexible manner, illustrating how a protein can interact with DNAs containing targets of different sequences.},
note = {0021-9258
Journal Article},
keywords = {Amino Acid Sequence Animals Binding Sites DNA-Binding Proteins/chemistry/*metabolism Deoxyribonuclease I/pharmacology Human Molecular Sequence Data *Promoter Regions (Genetics) RNA, Amino Acid-Specific/*genetics Support, Non-U.S. Gov't Trans-Activators/chemistry/*metabolism Xenopus *Zinc Fingers, Small Nuclear/*genetics RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1994
Meissner W, Wanandi I, Carbon P, Krol A, Seifart K H
Transcription factors required for the expression of Xenopus laevis selenocysteine tRNA in vitro Article de journal
Dans: Nucleic Acids Res, vol. 22, no. 4, p. 553-559, 1994, ISBN: 8127703, (0305-1048 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Amino Acid-Specific/*genetics Support, Animals Base Sequence DNA-Binding Proteins/*physiology Human Molecular Sequence Data Oligonucleotide Probes RNA, Genetic Xenopus laevis, Non-U.S. Gov't TATA Box Transcription Factors/*genetics Transcription, Transfer, Unité ARN
@article{,
title = {Transcription factors required for the expression of Xenopus laevis selenocysteine tRNA in vitro},
author = {W Meissner and I Wanandi and P Carbon and A Krol and K H Seifart},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8127703},
isbn = {8127703},
year = {1994},
date = {1994-01-01},
journal = {Nucleic Acids Res},
volume = {22},
number = {4},
pages = {553-559},
abstract = {It has previously been reported that transcription in vivo of the tRNA(Sec) gene requires three promoter elements, a PSE and a TATA-box upstream of the coding region which are functionally interchangeable with the U6 snRNA gene counterparts and an internal B-block, resembling that of classical tRNA genes (1). We have established an in vitro transcription system from HeLa cells in which three factors, which are either essential for or stimulate transcription were identified. Apart from the TATA-binding protein TBP, the PSE-binding protein PBP was found to be essentially required for expression of the gene. Depletion of PBP from cell extracts by PSE-oligonucleotides abolished tRNA(Sec) transcription, which could be reconstituted by readdition of partially purified PBP. Addition of increasing amounts of recombinant human TBP to an S100 extract stimulated transcription of the tRNA(Sec), the mouse U6 snRNA and the human Y3 genes, an effect which was not observed in the case of a TATA-less tRNA gene. Purified human TFIIA strongly stimulated tRNA(Sec) transcription in a fashion depending on the concentration of TBP. Surprisingly, partially purified TFIIIC was shown to be dispensable for transcription in vitro and unable to bind the B-block of this gene in vitro, although its sequence matches the consensus for this element. Collectively, these data suggest that the mechanism by which transcription complexes are formed on the tRNA(Sec) gene is dramatically different from that observed for classical tRNA genes and much more resembles that observed for externally controlled pol III genes.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid-Specific/*genetics Support, Animals Base Sequence DNA-Binding Proteins/*physiology Human Molecular Sequence Data Oligonucleotide Probes RNA, Genetic Xenopus laevis, Non-U.S. Gov't TATA Box Transcription Factors/*genetics Transcription, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}