I'm reading about pyoverdin, and I've decided it seems very similar to GFP.

 

Why were researchers in the past so focused on GFP as a marker in cells rather than pyoverdin?

 

Was it that GFP better enabled itself to be embedded in proteins rather than be used an a gene insert?

I'm reading about pyoverdin, and I've decided it seems very similar to GFP.

 

Your decision is wrong. Pyoverdine is very different from GFP. It isn't even a protein and thus unsuited for basically all kind of experiments in which GFP is used. You have to read more carefully before coming to any conclusions.

Edited June 24, 201015 yr by CharonY

Your decision is wrong. Pyoverdine is very different from GFP. It isn't even a protein and thus unsuited for basically all kind of experiments in which GFP is used. You have to read more carefully before coming to any conclusions.

 

Right. Ok, not a protein as such an item would be relevant to gene transcription (and the structure of both molecules is different, because one is composed of amino acids and the other isn't).

 

But how about taking the operon that leads to the production of pyoverdin?

That wouldn't work, because it couldn't be part of the protein, right?

 

I'm guessing it shouldn't been seen as a competitor in any way to GFP?

 

Either way, both glow. I think their glowiness is their most important aspect. It looks pretty.

A lot of stuff is fluorescent. But that is not where the usefulness of the GFP comes in. Think about the uses of GFP and now try to but that into context of pyverdine synthesis.

Ok, inserting of the GFP gene at decent locations in the protein's gene enable the GFP gene to be used as a marker. If the genes for pyoverdin were inserted there, it's just f@#$ up the whole process and make the protein way larger than it needs to be, thus leading to a nonfunctional protein.

 

What I'm reading, though, is that one thing that became of importance is that pyoverdin is phototoxic, unlike GFP.