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Ku70-binding protein/assembly of the F0 sector of the F1F0 ATP synthase complex?/annot query

Valerie Wood val at sanger.ac.uk
Mon Apr 2 06:21:02 PDT 2007



Some proteins in Uniprot and the MODs appear to be annotated as 
Ku70-binding protein, (possibly from the KOGs annotation?).

However, this appears to be involved in assembly of the F0 sector of the 
F1F0 ATP synthase complex 
(see details in Pfam submission below)


You can see some of the affected gene products here:

http://www.sanger.ac.uk/cgi-bin/PostGenomics/S_pombe/YOGY/yogy-search.pl?gene=SPCC320.12&species=S._pombe&wild=No&go_term=No&go_final=No

or here:

http://www.sanger.ac.uk/cgi-bin/Pfam/getallproteins.pl?name=Pfam-B_10086&acc=PB010086&type=full&verbose=true&zoom_factor=0.5&list=View+Graphic

If anybody has any experimantal basis for Ku binding, can they let me know and I'll update the Pfam submission.

Thanks



------------------------------
ATP23

>From SGD annotation:
Putative metalloprotease of the mitochondrial inner membrane, required for processing of Atp6p; has an additional role in assembly of the F0 sector of the F1F0 ATP synthase complex. The peptidase activity is also supported Interpro hit to IPR006025	

This protein is sometimes annotated as a Ku-binding protein DNA-dependent protein kinase or double-strand break repair via nonhomologous end
joining in metazoans (in human, drosophila mouse), but usually these appear to be inferred from sequence similarity or traceable author statements. I haven't been able to trace any experimental evidence for any of these annotations.
The peptidase activity is also supported Interpro hit to IPR006025	

I suppose the other reported annotations could be correct but as this is conserved one copy per organism this would be unusual.

PMID: 17135290


Val


-- -- 
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Valerie Wood			 Tel: 01223 496909
S. pombe Genome Project		 Fax: 01223 494919 		       
Wellcome Trust Sanger Institute	 email: val at sanger.ac.uk
Wellcome Trust Genome Campus	 http://www.genedb.org/genedb/pombe 
Hinxton, Cambridge, CB10 1HH	 http://www.sanger.ac.uk/Projects/S_pombe




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