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TFTC is structurally similar to TFIID [10], [11], and although devoid of TBP, it is capable of functionally replacing TFIID at both TATA-containing and TATA-less promoters in vitro [7].
Since the authors orient the insertions toward TBP, it is likely that TBP would be "pushed" rather than "pulled", assuming that TBP translocates before disruption.
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On a similar note, it has been proposed that in cells heterozygous for TBP (tbp +/-), elevated levels of TBP2 compensate abnormally low levels of TBP at some but not all promoters [ 32].
This concentration is measured by the TBP and it is bounded by [14, page 50] (9).
For example, MGBDs have been shown to compete with the transcription factor NF-Y for binding to the DNA minor groove [ 23] and to both prevent and disrupt binding of TBP to it [ 24].
Although we have no evidence that these complexes are functional in the LBP or TBP fractions, it is possible that other isozymes replace deficient ones, as shown in this study.
The very organization of the Amy32b gene 5' area appears to be favourable for TBP binding, as it contains several inverted sequences [ 16], but it was shown that repeated sequences are often found in the TBP anchoring sites [ 3- 6].
While Mot1 forms a stable complex with DNA-bound TBP and NC2, it is fully capable of disrupting this complex in the presence of ATP.
Even though TBP is essential, it is necessary for transcription of only a small subset of genes in Xenopus embryos [ 56].
The mouse Pdcd2 gene has been mapped to mouse chromosome (Chr) 17, tail-to-tail to the gene for TATA-binding protein (Tbp), which makes it a candidate for the mouse Hst1 gene [ 1, 2].
In yeast the binding of Gcn4 to Mbf1 was not altered by a D112A mutation (Tbp binding), but it was slightly reduced by the N-terminal deletion of yMbf1 (MBF1ΔNT).
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