Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We reported previously that cell-free transcription in the Archaea Methanococcus and Pyrococcus depends upon two archaeal transcription factors, archaeal transcription factor A (aTFA) and archaeal transcription factor B (aTFB). In the genome of Pyrococcus genes encoding putative homologues of eucaryal transcription factors TATA-binding protein (TBP) and TFIIB have been detected. Here, we report that Escherichia coli synthesized Pyrococcus homologues of TBP and TFIIB are able to replace endogenous aTFB and aTFA in cell-free transcription reactions. Antibodies raised against archaeal TBP and TFIIB bind to polypeptides of identical molecular mass in the aTFB and aTFA fraction. These data identify aTFB as archaeal TBP and aTFA as the archaeal homologue of TFIIB. At the Pyrococcus glutamate dehydrogenase (gdh) promoter these two bacterially produced transcription factors and endogenous RNA polymerase are sufficient to direct accurate and active initiation of transcription. DNase I protection experiments revealed Pyrococcus-TBP producing a characteristic footprint between position -20 and -34 centered around the TATA box of gdh promoter. Pyrococcus-TFIIB did not bind to the TATA box but bound cooperatively with Pyrococcus-TBP generating an extended DNase I footprinting pattern ranging from position -19 to -42. These data suggest that the Pyrococcus homologue of TFIIB associates with the TBP-promoter binary complex as its eucaryal counterpart, but in contrast to eucaryal TFIIB, it causes an extension of the protection to the region upstream of the TATA box.
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PMID:Two transcription factors related with the eucaryal transcription factors TATA-binding protein and transcription factor IIB direct promoter recognition by an archaeal RNA polymerase. 893 64

Protein motifs represent highly conserved regions within protein families and are generally accepted to describe critical regions required for protein stability and/or function. In this comprehensive analysis, we present a robust, unique approach to identify and compare corresponding mesophilic and thermophilic sequence motifs between all orthologous proteins within 44 microbial genomes. Motif similarity is determined through global sequence alignment of mesophilic and thermophilic motif pairs, which are identified by a greedy algorithm. Our results reveal only modest correlation between motif and overall sequence similarity, highlighting the rationale of motif-based approaches in comprehensive multigenome comparisons. Conserved mutations reflect previously suggested physiochemical principles for conferring thermostability. Additionally, comparisons between corresponding mesophilic and thermophilic motif pairs provide key biochemical insights related to thermostability and can be used to test the evolutionary robustness of individual structural comparisons. We demonstrate the ability of our unique approach to provide key insights in two examples: the TATA-box binding protein and glutamate dehydrogenase families. In the latter example, conserved mutations hint at novel origins leading to structural stability differences within the hexamer structures. Additionally, we present amino acid composition data and average protein length comparisons for all 44 microbial genomes.
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PMID:Using motif-based methods in multiple genome analyses: a case study comparing orthologous mesophilic and thermophilic proteins. 1288 31