Publications
1993
Myslinski E, Schuster C, Huet J, Sentenac A, Krol A, Carbon P
Point mutations 5' to the tRNA selenocysteine TATA box alter RNA polymerase III transcription by affecting the binding of TBP Journal Article
In: Nucleic Acids Res, vol. 21, no. 25, pp. 5852-5858, 1993, ISBN: 8290344, (0305-1048 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid-Specific/*genetics/metabolism Recombinant Proteins/metabolism Support, Animals Base Sequence DNA/metabolism DNA-Binding Proteins/*metabolism Molecular Sequence Data *Point Mutation Protein Binding RNA Polymerase III/*metabolism RNA, Genetic Xenopus laevis, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factors/*metabolism *Transcription, Transfer, Unité ARN
@article{,
title = {Point mutations 5' to the tRNA selenocysteine TATA box alter RNA polymerase III transcription by affecting the binding of TBP},
author = {E Myslinski and C Schuster and J Huet and A Sentenac and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8290344},
isbn = {8290344},
year = {1993},
date = {1993-01-01},
journal = {Nucleic Acids Res},
volume = {21},
number = {25},
pages = {5852-5858},
abstract = {The selenocysteine tRNA(Sec) gene possesses two external promoter elements, one of which is constituted by a strong TATA box. Point mutant analysis performed in this study led to the conclusion that the functional TATA promoter actually encompasses the sequence -34 GGGTATAAAAGG-23. Individual changes at T-31 do not affect transcription much. Position T-29 is less permissive to mutation since transversion to a G, for example, is less well tolerated than at T-31. Interestingly, a double point mutation, converting GG(-33/-32) to TT, causes abrogation of transcription in vivo and severe reduction of transcription in vitro with human TBP. Therefore, data obtained underscore the fact that, in the Xenopus tRNA(Sec), these two Gs are an integral part of the TATA promoter. Gel retardation experiments indicate that the GG to TT substitution, which led human TBP to lose its ability to support efficient transcription in vitro, correlates with the appearance of an altered pattern of retarded complexes. Altogether, the data presented in this report support a model in which TBP interacts directly with the TATA element of the tRNA(Sec) gene, in contrast to the type of interaction proposed for classical TATA-less tRNA genes.},
note = {0305-1048
Journal Article},
keywords = {Amino Acid-Specific/*genetics/metabolism Recombinant Proteins/metabolism Support, Animals Base Sequence DNA/metabolism DNA-Binding Proteins/*metabolism Molecular Sequence Data *Point Mutation Protein Binding RNA Polymerase III/*metabolism RNA, Genetic Xenopus laevis, Non-U.S. Gov't *TATA Box TATA-Box Binding Protein Transcription Factors/*metabolism *Transcription, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}