marismortui’s two pch proteins, pch1 and pch2, are structurally very similar and in fact both contain a TrkA N-domain (Figure A and D) (Mitchell, et al. 2015). Despite these similarities, both show dissimilar expression patterns in Har. marismortui under low potassium stress conditions (20mM potassium) after acclimatization at normal potassium levels (120mM potassium). When experiencing low potassium shock, pch1 mRNA has a large expression spike 4 hours after introduction to new conditions compared to pch2, which does not show a significant change in expression at any time interval or potassium level (Short, et al. 2016). Despite similarities between the pch proteins, pch1 originates on a plasmid within Har. marismortui, and pch2 is chromosomal, these differences, as well as the figure B low potassium expression data point to pch1 and pch2 playing different roles in Har. marismortui, details of their roles are unknown at present. Interestingly, pch1 and pch2 both contain a TrkA N
marismortui’s two pch proteins, pch1 and pch2, are structurally very similar and in fact both contain a TrkA N-domain (Figure A and D) (Mitchell, et al. 2015). Despite these similarities, both show dissimilar expression patterns in Har. marismortui under low potassium stress conditions (20mM potassium) after acclimatization at normal potassium levels (120mM potassium). When experiencing low potassium shock, pch1 mRNA has a large expression spike 4 hours after introduction to new conditions compared to pch2, which does not show a significant change in expression at any time interval or potassium level (Short, et al. 2016). Despite similarities between the pch proteins, pch1 originates on a plasmid within Har. marismortui, and pch2 is chromosomal, these differences, as well as the figure B low potassium expression data point to pch1 and pch2 playing different roles in Har. marismortui, details of their roles are unknown at present. Interestingly, pch1 and pch2 both contain a TrkA N