The linker domain of basal transcription factor TFIIB controls distinct recruitment and transcription stimulation functions

RNA polymerases (RNAPs) require basal transcription factors to assist them during transcription initiation. One of these factors, TFIIB, combines promoter recognition, recruitment of RNAP, promoter melting, start site selection and various post-initiation functions. The ability of 381 site-directed mutants in the TFIIB ‘linker domain’ to stimulate abortive transcription was systematically quantitated using promoter-independent dinucleotide extension assays. The results revealed two distinct clusters (mjTFIIB E78-R80 and mjTFIIB R90-G94, respectively) that were particularly sensitive to substitutions. In contrast, a short sequence (mjTFIIB A81-K89) between these two clusters tolerated radical single amino acid substitutions; short deletions in that region even caused a marked increase in the ability of TFIIB to stimulate abortive transcription (‘superstimulation’). The superstimulating activity did, however, not correlate with increased recruitment of the TFIIB/RNAP complex because substitutions in a particular residue (mjTFIIB K87) increased recruitment by more than 5-fold without affecting the rate of abortive transcript stimulation. Our work demonstrates that highly localized changes within the TFIIB linker have profound, yet surprisingly disconnected, effects on RNAP recruitment, TFIIB/RNAP complex stability and the rate of transcription initiation. The identification of superstimulating TFIIB variants reveals the existence of a previously unknown rate-limiting step acting on the earliest stages of gene expression

TFIIB aptamers inhibit transcription by perturbing PIC formation at distinct stages

Transcription in eukaryotes is a multistep process involving the assembly and disassembly of numerous inter- and intramolecular interactions between transcription factors and nucleic acids. The roles of each of these interactions and the regions responsible for them have been identified and studied primarily by the use of mutants, which destroy the inherent properties of the interacting surface. A less intrusive but potentially effective way to study the interactions as well as the surfaces responsible for them is the use of RNA aptamers that bind to the interacting factors. Here, we report the isolation and characterization of high-affinity RNA aptamers that bind to the yeast general transcription factor TFIIB. These aptamers fall into two classes that interfere with TFIIB's interactions with either TBP or RNA polymerase II, both of which are crucial for transcription in yeast. We demonstrate the high affinity and specificity of these reagents, their effect on transcription and preinitiation complex formation and discuss their potential use to address mechanistic questions in vitro as well as in vivo

Properties of Bread Dough with Added Fiber Polysaccharides and Phenolic Antioxidants: A Review

During breadmaking, different ingredients are used to ensure the development of a continuous protein network that is essential for bread quality. Interests in incorporating bioactive ingredients such as dietary fiber (DF) and phenolic antioxidants into popular foods such as bread have grown rapidly, due to the increased consumer health awareness. The added bioactive ingredients may or may not promote the protein cross-links. Appropriate cross-links among wheat proteins, fiber polysaccharides, and phenolic antioxidants could be the most critical factor for bread dough enhanced with DF and phenolic antioxidants. Such cross-links may influence the structure and properties of a bread system during baking. This article presents a brief overview of our current knowledge of the fate of the key components (wheat proteins, fibers, and phenolic antioxidants) and how they might interact during bread dough development and baking

ESG data

ESG Data</p

S&amp;P BSE Healthcare Data

Data of S&amp;P BSE Healthcare Index, Collected from Bombay stock exchange of IndiaTHIS DATASET IS ARCHIVED AT DANS/EASY, BUT NOT ACCESSIBLE HERE. TO VIEW A LIST OF FILES AND ACCESS THE FILES IN THIS DATASET CLICK ON THE DOI-LINK ABOV