Publications
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 Journal Article
In: J Biol Chem, vol. 274, no. 34, pp. 24241-24249, 1999, ISBN: 10446199, (0021-9258 Journal Article).
Abstract | Links | BibTeX | Tags: 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}
}
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.