Talk:Subfunctionalization

Untitled
Is there any chance you could add some examples of subfunc? Also, could you talk about its evolutionary importance? EricBakota (talk) 00:18, 16 February 2011 (UTC)

Format of references
There were two copies of references so I just removed one copy. The section title should be named as References but not Notes since the references are listing in this section. External links were added to the references. Format were changed a bit to reach the requirements. Bingjun Zhang (talk) 23:56, 14 February 2011 (UTC)

It would be helpful to see a clearer conceptual transition between (or explanation connecting) the second and third sentences.Laraappleby (talk) 03:53, 17 February 2011 (UTC)

hemoglobin
Hemoglobin's oligomeric architecture is not a case of subfunctionalization. It's alpha and beta chains evolved from a gene duplication event of ancestral, uncooperative dimer. Both chains in isolation retain the ability to form these dimers, but the beta chain in addition can form homotetramers. When both chains are mixed, they form the familiar a2b2 heterotetramer. Hemoglobin's ability to bind oxygen cooperatively emerged only after the duplication and is tied to the emergence of tetramers. It thus represents neofunctionalization. No aspect of the protein subfunctionalized according to current knowledge, because both the alpha and beta chain retain the two pertinent features of their ancestor: oxygen binding and dimerization. See here for details. https://www.nature.com/articles/s41586-020-2292-y (I am an author on this study)

Other aspects of hemoglobin may be due to subfunctionalization (for example differential expression patterns of its various isoforms).

Georg Hochberg

137.248.1.6 (talk) 07:38, 18 January 2021 (UTC)