Publications
2004
Myslinski E, Krol A, Carbon P
Characterization of snRNA and snRNA-type genes in the pufferfish Fugu rubripes Journal Article
In: Gene, vol. 330, pp. 149-158, 2004, ISBN: 15087134, (0378-1119 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Sequence Homology, Complementary/chemistry/genetics DNA-Binding Proteins/metabolism Female Genome Molecular Sequence Data Oocytes/metabolism Promoter Regions (Genetics)/genetics Protein Binding RNA, DNA Sequence Homology, KROL Amino Acid Sequence Animals Base Sequence Binding Sites/genetics Comparative Study DNA, Nucleic Acid Takifugu/*genetics Transcription Factors/metabolism Xenopus laevis, Nucleic Acid/genetics Response Elements/genetics Sequence Alignment Sequence Analysis, Small Nuclear/*genetics Regulatory Sequences, Unité ARN
@article{,
title = {Characterization of snRNA and snRNA-type genes in the pufferfish Fugu rubripes},
author = {E Myslinski and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15087134},
isbn = {15087134},
year = {2004},
date = {2004-01-01},
journal = {Gene},
volume = {330},
pages = {149-158},
abstract = {Vertebrate snRNA and snRNA-type genes occur in independent transcription units with external promoters. The transcription level from the basal promoter is enhanced by the distal sequence element DSE. This element contains almost invariably two activator submotifs, the Staf binding site and the octamer motif, recruiting the Staf and Oct-1 transcriptional activators. In the present work, database search identified 35 snRNA and snRNA-type genes in the genome sequence of the pufferfish Fugu rubripes. Sequence comparisons of promoter elements, determination of template activities by microinjection into Xenopus oocytes and DNA binding assays of the transcriptional activators led to the surprising finding that only two Fugu genes conform to the general scheme with the expected two submotifs in the DSE. Distinctively, all the other DSEs harbor a unique Staf binding site. Also striking was the observation that the tRNA(Sec), and the snRNA genes that are tandemly repeated, are transcribed from promoter-less DSEs. Evolutionary implications of these results are discussed.},
note = {0378-1119
Journal Article},
keywords = {Amino Acid Sequence Homology, Complementary/chemistry/genetics DNA-Binding Proteins/metabolism Female Genome Molecular Sequence Data Oocytes/metabolism Promoter Regions (Genetics)/genetics Protein Binding RNA, DNA Sequence Homology, KROL Amino Acid Sequence Animals Base Sequence Binding Sites/genetics Comparative Study DNA, Nucleic Acid Takifugu/*genetics Transcription Factors/metabolism Xenopus laevis, Nucleic Acid/genetics Response Elements/genetics Sequence Alignment Sequence Analysis, Small Nuclear/*genetics Regulatory Sequences, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
2002
Lescure A, Allmang C, Yamada K, Carbon P, Krol A
cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2 Journal Article
In: Gene, vol. 291, no. 1-2, pp. 279-285, 2002, ISBN: 12095701, (0378-1119 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN
@article{,
title = {cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2},
author = {A Lescure and C Allmang and K Yamada and P Carbon and A Krol},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12095701},
isbn = {12095701},
year = {2002},
date = {2002-01-01},
journal = {Gene},
volume = {291},
number = {1-2},
pages = {279-285},
abstract = {Selenocysteine and selenoprotein synthesis require a complex molecular machinery in mammals. Among the key players is the RNA-protein complex formed by the selenocysteine insertion sequence (SECIS) binding protein (SBP2) and the SECIS element, an RNA hairpin in the 3' untranslated regions of selenoprotein messenger RNAs (mRNAs). We have isolated the DNA complementary to mRNA of the human SBP2, enabling us to establish that it differs from a previously reported human SBP2-like protein. Examination of the expression pattern revealed that the human SBP2 protein is encoded by a 4 kb long mRNA that is over-expressed in testis. Compared to the rat SBP2 sequence, the human SBP2 protein displays two highly conserved domains with 92 and 95% amino acid identity, the latter one containing the RNA binding domain. The inter-domain section carries 55% sequence identity, the remainder of the SBP2 sequences showing about 65% identity, values lower than expected for two mammalian proteins. Interestingly, we could show that the binding of human SBP2 to the SECIS RNA is stimulated by the selenoprotein-specialized elongation translation factor mSelB/eEFsec.},
note = {0378-1119
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Blotting, Complementary/chemistry/genetics Female Gene Expression Human Male Molecular Sequence Data Peptide Elongation Factors/metabolism Protein Binding RNA/*metabolism RNA, DNA Sequence Homology, ERIANI, LESCURE, Messenger/genetics/metabolism RNA-Binding Proteins/genetics/*metabolism Sequence Alignment Sequence Analysis, Molecular DNA, Non-U.S. Gov't, Northern Cloning, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
1995
Schuster C, Myslinski E, Krol A, Carbon P
Staf, a novel zinc finger protein that activates the RNA polymerase III promoter of the selenocysteine tRNA gene Journal Article
In: EMBO J, vol. 14, no. 15, pp. 3777-3787, 1995, ISBN: 7641696, (0261-4189 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Animals Base Sequence Cloning, Amino Acid-Specific/*genetics Recombinant Fusion Proteins/metabolism Sequence Analysis, DNA Sequence Homology, Messenger RNA, Molecular DNA/metabolism DNA-Binding Proteins/biosynthesis/genetics/*metabolism Gene Expression Genes, Non-U.S. Gov't Trans-Activation (Genetics)/*physiology Trans-Activators/biosynthesis/genetics/*metabolism Xenopus laevis *Zinc Fingers, Reporter Human Molecular Sequence Data Oocytes Promoter Regions (Genetics)/*genetics RNA Polymerase III/*genetics RNA, Transfer, Unité ARN
@article{,
title = {Staf, a novel zinc finger protein that activates the RNA polymerase III promoter of the selenocysteine tRNA gene},
author = {C Schuster and E Myslinski and A Krol and P Carbon},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7641696},
isbn = {7641696},
year = {1995},
date = {1995-01-01},
journal = {EMBO J},
volume = {14},
number = {15},
pages = {3777-3787},
abstract = {The selenocysteine tRNA gene (tRNA(Sec)) is atypical. Though transcribed by RNA polymerase III like all other tRNA genes, its basal promoter elements are distinct and reside essentially upstream of the coding region. In addition, transcription from the basal promoter is activated by a 15 bp activator element. In this report we describe the cloning and functional characterization of Staf (selenocysteine tRNA gene transcription activating factor), a novel Xenopus laevis transcription factor which binds to the tRNA(Sec) activator element and mediates its activation properties. The 600 amino acid Staf protein contains seven zinc fingers and a separate acidic activation domain. Seven highly conserved regions were detected between Staf and human ZNF76, a protein of unknown function, thereby aiding in predicting the locations of the functional domains of Staf. With the use of a novel expression assay in X.laevis oocytes we succeeded in demonstrating that Staf can activate the RNA polymerase III promoter of the tRNA(Sec) gene. This constitutes the first demonstration of the capacity of a cloned factor to activate RNA polymerase III transcription in vivo.},
note = {0261-4189
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Animals Base Sequence Cloning, Amino Acid-Specific/*genetics Recombinant Fusion Proteins/metabolism Sequence Analysis, DNA Sequence Homology, Messenger RNA, Molecular DNA/metabolism DNA-Binding Proteins/biosynthesis/genetics/*metabolism Gene Expression Genes, Non-U.S. Gov't Trans-Activation (Genetics)/*physiology Trans-Activators/biosynthesis/genetics/*metabolism Xenopus laevis *Zinc Fingers, Reporter Human Molecular Sequence Data Oocytes Promoter Regions (Genetics)/*genetics RNA Polymerase III/*genetics RNA, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}