Say I have one gene transcript that encodes for two proteins in a cell line. The first 1/3 of the transcript encodes for the first protein ("small" protein) and the last 2/3 encodes for the second protein ("large" protein).
I tested this gene transcript in a cell line under normal and stress conditions. I also made separate transcripts where I could test just the first 1/3 of the transcript and the last 2/3, thereby isolating both proteins from each other, basically trying to see if there were any differences seen by individually encoding them.
My results were that when both proteins were encoded by the gene transcript, the cell was stress tolerant (viable, healthy). When just the small protein was encoded, the same was seen. But when just the large protein was encoded, the cell was stress sensitive (decrease in size, somewhat functional but not much). So there is a difference seen in the cell when the proteins are individually encoded.
Of course, I am thinking, well there is something else in the large protein that confers the cell stress sensitive. But as you remember from above, when both proteins were encoded, the cell was stress tolerant.
So I am wondering why the difference when the protein is isolated? I already checked it by in vitro and I know the two proteins are encoding separately.
Has anyone run across this kind of research in proteomics, where if the two proteins are encoded together, they show a specific response under one condition, but when one of the proteins is isolated, it shows the opposite response under the same condition?
If I could be directed towards some papers that would even be helpful!
Edited by claritylight, 06 April 2009 - 04:19 PM.