Is there anyone who can help me in characterising a novel protein with interesting domain fusion. Excellent wet lab experimental data is there... Discussion wrt evolution and significance is needed. Authorship open for Genuine help.
Hi Timir, can you divulge any information about the function of your protein?
Hi Tamir, could you expand on the system, problem you want to address, and data you've got?
Dear Tamir,
I'm also interested for discussion on this, but as the two previous fellows mentioned, I need more informations...
Waiting from your side
Best
Guillaume
Thanks for having interest in my work…
Here is the problem…
We work on redox active proteins of parasite- liver fluke.. right now the work is with a protein- Glutaredoxin (Grx)…. Grx contain a conserved thioredoxin fold.
Grx is generally a single domain protein, which exists as monomer, dimer or tetramer. Sometimes Grx can exist in 2 domain form, with one more different domain, means one Grx and one some other domain….
Now we have interesting situation. Blasting the sequence of our Grx results into two putative “thioredoxin folds” suggesting a gene fusion event in our organism. We will report for the first time that two Grx domains are fused together in one protein….. Interestingly, an alignment of the first and second part of Grx (Domain= D1 and D2) with Plasmodium falciparum dithiol glutaredoxin 1 (PfGrx1) and three monothiol glutaredoxins from this parasite (PfGLP1, 2, and 3) showed a closer similarity of FgGrxD1 to the dithiol PfGrx1, although it contains only one active site cysteine residue homologue. D2 of FgGrx is more similar to the monothiol Grx of Plasmodium. This led us to analyse if the two domains may have evolved differently and we therefore cloned them independently for further testing. We did have all wet lab data (activity/oligomerization/S-glutathionylation etc) with full length and the D1 and D2.
Now we want to characterize evolutionarily that what is the significance of this novel domain fusionand why did this phenomenon happened in nature. We don’t have that much expertise to do bioinformatics analysis, so I m seeking help.
Hi Timir,
Domain's are in a way independent units of evolution, and they can fuse. What you have found for your case, is not rare.
Have a look, for a recent review, at:
E. Bornberg-Bauer and M.Mar Alba; Dynamics and Adaptive Benefits of Modular Protein Evolution, Curr Opn Struct Biol 2013.
Cheers,
Julian
Dear Timir,
Thank you for the informations you provided.
I think at least you can do a molecular phylogeny with the blast results on both D1 and D2. That can give a better idea of the evolutionary relationships.
After, have you characterized the entire sequence of the gene (by genome walking or if genome is already published)?. It can be interesting to understand how the second domain becomes a fusion of D1 at the genetic level. Maybe bring you some information on the origin of the second domain.
Hope this will help you...
Best
Guillaume
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