My questions/comments:
 * Do you plan to express the fusion proteins from plasmids for the 
localization studies? If the goal is to understand native localization, I would 
be cautious with overexpression and consider tagging the proteins at their 
endogenous chromosomal loci instead. * Would it be useful to first confirm the 
protein–protein interaction in vivo? For example, a split NanoLuc/NanoBiT 
approach could provide evidence that the interaction occurs inside the cell 
while minimizing the size of the tag. * Have you considered using a small 
split-GFP tag such as GFP11? This could potentially allow localization of the 
proteins with minimal perturbation. You could also consider localizing both 
proteins separately; if they are found in the same cellular compartment and the 
interaction is independently confirmed in vivo, that may provide a strong 
overall picture. * One point to keep in mind with GFP complementation 
approaches is that the reconstituted fluorescence can be stable and may not 
always represent the exact real-time location of the interaction event, so 
interpretation of the localization signal would need to be done carefully.



On Monday, July 06, 2026 06:53 CEST, Harshitha H N 
<[email protected]> wrote:

 
I am designing a bacterial protein interaction and co-localisation study 
involving two interacting proteins.
One protein is very small (~7–8 kDa), while the other is approximately 25–30 
kDa. Previous biochemical experiments (crystal structure and binding studies) 
have confirmed that the two proteins interact, and one protein modulates the 
function of the other.
My initial plan was to generate fluorescent protein fusions (EGFP and mCherry) 
for live-cell co-localisation. However, I am concerned that fusing a ~27–29 kDa 
fluorescent protein to the smaller protein may interfere with its folding, 
localisation, or interaction.

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