The sequenced partial IGR spanned 311 nt and contained stretches highly rich in A and U residues, which is typical for the IGRs of tospoviral S RNA segments.
The probability (percent of experiments or cells with Ca2+ sparks) and frequency of Ca2+ release events induced by stretch were highly related to both the degree of stretch and the time that stretch was maintained.
A stretch of highly basic amino acid residues is also found in the chicken GnRH receptor (RKRRK) at the equivalent region in the first intracellular loop (Fig. 3A, Table 1), however, similar sequences are not located in any part of the mammalian type II GnRH-R (data not shown), a receptor that appears to be activated only by the type II GnRH.
This is all in agreement with empirical studies that show the polarization of the C2=O moiety, and hence the C2=O stretch, is highly correlated with chemical activity.
This stretch is highly divergent, indeed absent in some EssB orthologues, as evidenced by a multiple sequence alignment (Supplementary Figure S2 at http://www.biochemj.org/bj/449/bj4490469add.htm).htm
Since we consider only tandem duplications in our full model, the process has the potential to create an expanding stretch of highly neutral elements.
The long stretch of highly methylated DNA in the beginning is characterized by a high number of short pauses as well as the non-chord note sequences that correspond to patterns with only one unmethylated CpG site.
Essential for keeping the protein in this conformation is a short stretch of highly conserved amino acids that inhibits the transcriptional activity of TAp63 α by directly binding to other p63 domains.
The sequence of this short helix overlaps with the 'linker region' (Wengler, 2009), a stretch of highly conserved residues (109 125 for VEEV, Supplementary Figure S6) that binds to cellular 60S ribosomal subunits, which function to disassemble the nucleocapsid cores after they are released into the cytosol (Wengler et al, 1992).
The C-terminal region contains some amino acids which are conserved in Vas orthologues in other Drosophila species and terminates with a stretch of highly acidic residues, conserved in Vas orthologues in Drosophila and beyond, but not in other DEAD-box helicases.
