Sentence examples for modifying complexes are from inspiring English sources

However, it is still not understood how ubiquitously expressed chromatin modifying complexes are 'guided' to specific genomic sites to induce intricate patterns of epigenetic modifications.

However it is still unclear how these and other histone modifying complexes are recruited to specific gene targets in ES cells.

In general, a key question is how histone modifying complexes are selectively and timely recruited to promoters, and binding of sequence-specific transcription factors offers a convenient explanation [11] [16].

In both cases, a direct role for the lncRNA in targeting the histone modifying complexes was proposed, based on the findings that the lncRNAs interact with the respective histone modifying complex.

However, if Ras/RTK signaling is hyperactivated, or, as described below, if chromatin-modifying complexes are deregulated, additional precursor cells may be induced, leading to the formation of extra pseudovulvae.

For example, it is still not understood what distinguishes TAF-dependent and TAF-independent promoters in yeast (Kuras et al., 2000; Li et al., 2000), why some basic transcription factors, such as mediator, are bound at only some promoters (Fan et al., 2006), or the basis by which chromatin-modifying complexes are selectively recruited to promoters (Ng et al., 2002).

A major gap in our understanding of epigenetic regulation for chromatin-modifying complexes is how these complexes are targeted to specific regions of the genome.

The importance of these chromatin-modifying complexes is demonstrated by the fact that they are often conserved from yeast to humans (reviewed in [ 1- 3]).

Formation of the chromatin-modifying complex is dependent on dimerization of CtBPs, which is promoted by elevated levels of NADH in the cytosol and nuclei of cells.

Once Cys-39 of the ND3 subunit is modified, complex I is thought to be unable to undergo the D→A conversion and catalyse the physiological NADH ubiquinone reaction.

In addition, MBD-R2/NSL and Trx histone modifying complexes have been demonstrated to interact with full-length Nup98 in fly (Pascual-Garcia et al., 2014).