Identification of a mouse TBP-like protein (TLP) distantly related to the drosophila TBP-related factor.

TATA-binding protein (TBP) is an essential factor for eukaryotic transcription. In this study, we demonstrated a mouse cDNA encoding a 21 kDa TBP-like protein (TLP). The TLP ORF, carrying 186 amino acids, covered the entire 180 amino acids of the C-terminal conserved domain of mouse TBP with 39% identity and 76% similarity. Northern blot analysis demonstrated that TLP mRNAs were expressed in various mammalian tissues ubiquitously and that their distribution pattern was analogous to that of TBP. By using anti-TLP antibody, we demonstrated the existence of TLP proteins in various mammalian cells and tissues. The Drosophila TBP-related factor (TRF) is a neurogenesis-related transcription factor that binds to the TATA-box and activates transcription. TLP did not bind to the TATA-box nor direct transcription initiation. Multiple amino acids critical for TBP function were deleted or substituted in TLP, while amino acids in Drosophila TRF much resembled those in TBP. Similarity between Drosophila TRF and mouse TLP was considerably lower (alignment score 35) than that between Drosophila TBP and mouse TBP (alignment score 88). Identity of nucleotide sequences between mouse and putative human TLPs (94%) was higher than that between TBPs (91%) in these two animals. Expression of TLP was nearly constant throughout the P19 differentiation process. Accordingly, we suggest that, even if higher eukaryotes generally contain multiple tbp -related genes, TLP is not a bona fide mammalian counterpart of Drosophila TRF.

[1]  A. Hoffmann,et al.  Purification of his-tagged proteins in non-denaturing conditions suggests a convenient method for protein interaction studies. , 1991, Nucleic acids research.

[2]  R. Roeder,et al.  Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes , 1994, Cell.

[3]  W. Schaffner,et al.  Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. , 1989, Nucleic acids research.

[4]  J. Thompson,et al.  CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.

[5]  R. Roeder,et al.  Factors involved in specific transcription by human RNA polymerase II: analysis by a rapid and quantitative in vitro assay. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[6]  P. Lieberman,et al.  Cloning of a transcriptionally active human TATA binding factor. , 1990, Science.

[7]  Robert Tjian,et al.  Transcription Properties of a Cell Type–Specific TATA-Binding Protein, TRF , 1997, Cell.

[8]  P. Moore,et al.  Molecular cloning of the small (gamma) subunit of human TFIIA reveals functions critical for activated transcription. , 1994, Genes & development.

[9]  R. Conaway,et al.  Role of core promoter structure in assembly of the RNA polymerase II preinitiation complex. A common pathway for formation of preinitiation intermediates at many TATA and TATA-less promoters. , 1994, The Journal of biological chemistry.

[10]  S. Blatti,et al.  Purification using polyethylenimine precipitation and low molecular weight subunit analyses of calf thymus and wheat germ DNA-dependent RNA polymerase II. , 1977, Biochemistry.

[11]  M. Horikoshi,et al.  A bipartite DNA binding domain composed of direct repeats in the TATA box binding factor TFIID. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[12]  D. Reinberg,et al.  Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription , 1992, Cell.

[13]  S. Burley,et al.  Radical mutations reveal TATA-box binding protein surfaces required for activated transcription in vivo. , 1996, Genes & development.

[14]  S. Burley,et al.  Crystal structure of a TFIIB–TBP–TATA-element ternary complex , 1995, Nature.

[15]  M. Freeling,et al.  Expression of the two maize TATA binding protein genes and function of the encoded TBP proteins by complementation in yeast. , 1993, The Plant cell.

[16]  G. Zambetti,et al.  Wild-type p53 binds to the TATA-binding protein and represses transcription. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[17]  J. Hancock,et al.  Evolution of sequence repetition and gene duplications in the TATA-binding protein TBP (TFIID). , 1993, Nucleic acids research.

[18]  F. Young Biochemistry , 1955, The Indian Medical Gazette.

[19]  R. Roeder,et al.  The role of general initiation factors in transcription by RNA polymerase II. , 1996, Trends in biochemical sciences.

[20]  Masami Horikoshi,et al.  Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA box , 1989, Nature.

[21]  N. Hernandez,et al.  TBP, a universal eukaryotic transcription factor? , 1993, Genes & development.

[22]  M. Horikoshi,et al.  Sequence of general transcription factor TFIIB and relationships to other initiation factors. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[23]  M. Muramatsu,et al.  Multimerization of the mouse TATA-binding protein (TBP) driven by its C-terminal conserved domain. , 1994, Nucleic acids research.

[24]  F. Studier,et al.  Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.

[25]  M. Brand,et al.  Function of TAFII-containing complex without TBP in transcription by RNA polymerase II , 1998, Nature.

[26]  P. Sharp TATA-binding protein is a classless factor , 1992, Cell.

[27]  P. Sharp,et al.  Multiple sets of basal factors initiate transcription by RNA polymerase II. , 1994, The Journal of biological chemistry.

[28]  R. Tjian,et al.  Functional domains and upstream activation properties of cloned human TATA binding protein. , 1990, Science.

[29]  R. Tjian,et al.  Structure and functional properties of human general transcription factor IIE , 1991, Nature.

[30]  Robert Tjian,et al.  A new factor related to TATA-binding protein has highly restricted expression patterns in Drosophila , 1993, Nature.

[31]  C. S. Parker,et al.  cDNA clone encoding Drosophila transcription factor TFIID. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[32]  M. Muramatsu,et al.  Striking homology of the 'variable' N-terminal as well as the 'conserved core' domains of the mouse and human TATA-factors (TFIID). , 1991, Nucleic acids research.