Nucleic Acids Research, Vol 27, Issue 15 3146-3152, Copyright © 1999 by Oxford University Press
M Shimada, T Ohbayashi, M Ishida, T Nakadai, Y Makino, T Aoki, T Kawata, T Suzuki, Y Matsuda and T Tamura
TLP (TBP-like protein), which is a new protein dis-covered by us, has a
structure similar to that of the C-terminal conserved domain (CCD) of TBP,
although its function has not yet been elucidated. We isolated cDNA and
genomic DNA that encode chicken TLP (cTLP) and determined their structures.
The predicted amino acid sequence of cTLP was 98 and 91% identical to that
of its mammalian and Xenopus counterparts, respectively, and its
translation product was ubiquitously observed in chicken tissues. FISH
detection showed that chicken tlp and tbp genes were mapped at 3q2.6-2.8
and 3q2.4-2.6 of the same chromosome, respectively. Genome analysis
revealed that the chicken tlp gene was spliced with five introns.
Interestingly, the vertebrate tbp genes were also found to be split by five
introns when we focused on the CCDs, and their splicing points were similar
to those of tlp. On the contrary, another TBP-resembling gene of
Drosophila, trf1, is split by only one intron, as is the Drosophila 's tbp
gene. These results support our earlier assumption that vertebrate TLPs did
not directly descend from Drosophila TRF1. On the basis of these results
together with phylogenetical exam-ination, we speculate that tlp diverged
from an ancestral tbp gene through a process of gene duplication and point
mutations.
ARTICLES
Analysis of the chicken TBP-like protein(tlp) gene: evidence for a striking conservation of vertebrate TLPs and for a close relationship between vertebrate tbp and tlp genes
Department of Biology, Faculty of Science, Chiba University, CREST Japan Science and Technology Corporation, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan.
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