Wiki Education Foundation-supported course assignment

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  This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available on the course page. Student editor(s): Shadmort.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 06:35, 17 January 2022 (UTC)Reply

Attention from an expert?

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OK, I've spent an hour or two digging through the literature on the photolyase/cryptochrome family, and am still not certain whether active photolyases have been found in higher organisms than bacteria. There seems to be some mention, but there are also papers stating that higher organisms just have cryptochromes with sequence homology to photolyases and photosensitivity but no DNA repair activity. Could someone who works with these guys please clarify? -Kieran (talk) 20:25, 28 July 2010 (UTC)Reply

The mammalian CRY1 and CRY2 act as light-independent inhibitors of CLOCK-BMAL1 components of the circadian clock.Biophys (talk) 03:30, 3 November 2010 (UTC)Reply
Photolyases are present in bacteria, lower eucaryotes, plants and most animals. They have apparently been lost in placental mammals (e.g. man), but are present in insect (drosophila) , amphibian (xenopus) and even in marsupial mammals (kangaroos...)[1]. Transgenic mice expressing marsupial photolyase have been reported and they do have DNA repair activity : see for instance [2]. Cucumber and sorghum enzymes have also been characterized [3] and a photolyase from drosophila has been crystallized in complex with damaged DNA (PDB entry 3CVU), so its obviously not just bacteria.--Fdardel (talk) 16:14, 2 June 2011 (UTC)Reply

It looks to me like the primary question from Kierano was answered. I've removed the expert required tag.Pgholder (talk) 12:35, 12 September 2011 (UTC)Reply

drawing is incorrect

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the thymine molecule shown in the illustration is wrong. missing are the 5- methyl groups on the pyrimidine heterocycle lohselose

There exists a new theory

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The photolyase reactivation of pyrymidine dimer was assured, in several bacteria, by UR1C a deoxyribozyme. — Preceding unsigned comment added by 109.122.191.243 (talk) 18:57, 6 October 2013 (UTC)Reply