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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-6-15
pubmed:abstractText
TBPL2 is the most recently discovered and less characterized member of the TATA box binding protein (TBP) family that also comprises TBP, TATA box binding protein-like 1 (TBPL1), and Drosophila melanogaster TBP related factor (TRF). In this paper we report our in silico and in vitro data on (i) the genomics of the TBPL2 gene in Homo sapiens, Pan troglodytes, Mus musculus, Rattus norvegicus, Gallus gallus, Xenopus tropicalis, and Takifugu rubripes; (ii) its evolution and phylogenetic relationship with TBP, TBPL1, and TRF; (iii) the structure of the TBPL2 proteins that belong to the recently identified group of the intrinsically unstructured proteins (IUPs); and (iv) TBPL2 expression in different organs and cell types of Homo sapiens and Rattus norvegicus. Similar to TBP, both the TBPL2 gene and protein are bimodular. The 3' region of the gene encoding the DNA binding domain (DBD) was well conserved during evolution. Its high homology to vertebrate TBP suggests that TBPL2 also should bind to the TATA box and interact with the proteins binding to TBP carboxy-terminal domain, such as the TBP associated factors (TAFs). As already demonstrated for TBP, TBPL2 amino-terminal segment is intrinsically unstructured and, even though variable among vertebrates, comprises a highly conserved motif not found in any other known protein. Absence of TBPL2 from the genome of invertebrates and plants demonstrates its specific origin within the subphylum of vertebrates. Our RT-PCR analysis of human and rat RNA shows that, similar to TBP, TBPL2 is ubiquitously synthesized even though at variable levels that are at least two orders of magnitude lower. Higher expression of TBPL2 in the gonads than in other organs suggests that it could perform important functions in gametogenesis. Our genomic and expression data should contribute to clarify why TBP has a general master role within the transcription apparatus (TA), whereas both TBPL1 and TBPL2 perform tissue-specific functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1044-5498
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
369-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17570761-Amino Acid Sequence, pubmed-meshheading:17570761-Animals, pubmed-meshheading:17570761-Base Sequence, pubmed-meshheading:17570761-DNA Primers, pubmed-meshheading:17570761-Evolution, Molecular, pubmed-meshheading:17570761-Gene Expression, pubmed-meshheading:17570761-Genomics, pubmed-meshheading:17570761-Humans, pubmed-meshheading:17570761-Mice, pubmed-meshheading:17570761-Molecular Sequence Data, pubmed-meshheading:17570761-Nuclear Proteins, pubmed-meshheading:17570761-Phylogeny, pubmed-meshheading:17570761-Promoter Regions, Genetic, pubmed-meshheading:17570761-Protein Interaction Mapping, pubmed-meshheading:17570761-Rats, pubmed-meshheading:17570761-Sequence Homology, Amino Acid, pubmed-meshheading:17570761-TATA Box Binding Protein-Like Proteins, pubmed-meshheading:17570761-TATA-Box Binding Protein, pubmed-meshheading:17570761-Vertebrates
pubmed:year
2007
pubmed:articleTitle
Genomics, evolution, and expression of TBPL2, a member of the TBP family.
pubmed:affiliation
Dipartimento di Scienze Biomediche-Unità di Biologia Genetica e BioInformatica, Università di Catania, Catania, Italy, EU.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't