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Gordon Barker mjfasmb at fs1.ce.umist.ac.uk
Tue Oct 21 03:20:17 EST 1997

Dear Netters

I'm trying to maximise GFP-signal in my yeast cells to detect relatively low
levels of protein expressed from a weak promoter and consequently have a few
quick questions.  I've read on this newsgroup that people have successfully
fused 2 in-frame copies of GFP to produce an even brighter reporter
molecule.  Could anyone tell me what the optimal length of linker between
two such GFP monomers is ? and what (if any) are the amino-acid sequence
requirements ?  Or where I can even find this information ?
A major problem is likely to be signal-masking by the cell wall and
therefore another experiment I'm considering is to add a secretory signal to
GFP - does anybody know if there is a size limit on proteins to be secreted
from yeast ?

Thanks in advance !

 Gordon Barker
 Dept. of BioMolecular Sciences
 Sackville Street
 Manchester M60 1QD

 Tel: 0161 236 3311 ext. 2588
 Fax: 0161 236 0409

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