GO:0051289 "protein homotetramerization" only_in NCBITaxon:2759 "Eukaryota"
- Rule needs removing.
Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK.
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding. Biochemistry. 2008 Oct 7;47(40):10677-84. Epub 2008 Sep 11.
'The enzyme discussed here is a prokaryotic TDO from Xanthomonas campestris (the causative agent of black rot in cabbages), which shares 34% sequence identity with human TDO. The enzyme is a homotetramer that displays high substrate specificity, catalyzing the oxidation of l-Trp, 5-F-Trp, and 6-F-Trp (1).'
I have moved this back to cellular organisms.
Thanks,
Jen
Jen:
Isn't this a potentientally universal process?
Pascale
VIruses too you reckon? Shall I just remove the restriction then?
Jen
Jen,
I would remove it. You might want an opinion from a biochemist - but this is a basic property of proteins (to be able to dimerize, tetramerize, etc). For those process I think you're better off being 'generous' and allow all organisms - as far as I know, no specific process evolved to do this. One example Ifound is the HIV RT which is a heterodimer - I am sure there are many more of all sort of subunit arrangements.
Pascale
Hi Pascale,
It turns out that this term inherits the restriction from cellular component biogenesis and cellular component organisation which are both only_in_taxon cellular organisms. Shall I just remove both of these links? I'm not sure that we lose much.
Jen
I would remove the restrictions, yes.
Okay, will do. This is quite an interesting area actually. The whole virus thing has been really interesting in the way it affects the taxon rules. I have written down what I have found out on the wiki:
http://gocwiki.geneontology.org/index.php/Taxon-GO_Checks_and_Commentary_-_Part_4
In the meantime I will get rid of these restrictions.
Thanks,
Jen