Inositol, choline-responsive element gene transcriptions

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Associate Editor(s)-in-Chief: Henry A. Hoff

"When fused to the DNA-binding domain of [𝛃-galactosidase (Gal)] Gal4p, Ino2p but not Ino4p was able to activate a [upstream activation site] UASGAL-containing reporter gene even in the absence of the heterologous Fbfl subunit. By deletion studies, two separate transcriptional activation domains were identified in the N-terminal part of Ino2p. Thus, the [basic helix-loop-helix] bHLH domains of Ino2p and Ino4p constitute the dimerization/DNA-binding module of Fbfl mediating its interaction with the [inositol, choline-responsive element] ICRE, while transcriptional activation is effected exclusively by Ino2p."[1]

Human genes

Interactions

Consensus sequences

"This ICRE (consensus sequence TYTTCACATGY) contains the core sequence CANNTG, which is also known as an E box and which serves as a recognition site for DNA-binding proteins of the basic helix-loop-helix (bHLH) family (3). Members of the bHLH family comprise determinants of cellular differentiation and proliferation in mammalian and invertebrate systems such as the myogenic transcription factors MyoD, MRF4, myogenin and Myf-5(4) as well as factors not restricted to specialized tisues (E12, E47, daughterless, c-Myc and Mad; 5-7). Proteins of the bHLH group may form either homodimers or heterodimers or both, dependent on the individual structure of the respective interaction surface provided by the HLH domain(8)."[1]

Samplings

See also

References

  1. ↑ 1.0 1.1 Sabine Schwank, Ronald Ebbert, Karin Rautenstrau𝛃, Eckhart Schweizer and Hans-Joachim Schüller (25 January 1995). "Yeast transcriptional activator IN02 interacts as an Ino2p/Ino4p basic helix-loop-helix heteromeric complex with the inositol/choline responsive element necessary for expression of phospholipid biosynthetic genes in Saccharomyces cerevisiae" (PDF). Nucleic Acids Research. 23 (2): 230–37. doi:10.1093/nar/23.2.230. Retrieved 10 August 2020.

External links