Journal
DNA RESEARCH
Volume 18, Issue 1, Pages 39-52Publisher
OXFORD UNIV PRESS
DOI: 10.1093/dnares/dsq033
Keywords
circadian clock; His-Asp phosphorelay system; response regulator; pseudo-response regulator; Physcomitrella patens
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Funding
- Ministry of Education, Culture, Sports, Science and Technology Japan (MEXT)
- Japan Society for the Promotion of Science (JSPS) [21570005, 21780092]
- Grants-in-Aid for Scientific Research [21570005, 21780092] Funding Source: KAKEN
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The pseudo-response regulators (PRRs) are the circadian clock component proteins in the model dicot Arabidopsis thaliana. They contain a receiver-like domain (RLD) similar to the receiver domains of the RRs in the His Asp phosphorelay system, but the RLDs lack the phosphoacceptor aspartic acid residue invariably conserved in the receiver domains. To study the evolution of PRR genes in plants, here we characterize their homologue genes, PpPRR1, PpPRR2, PpPRR3 and PpPRR4, from the moss Physcomitrella patens. In the phylogenetic analysis, PpPRRs cluster together, sister to an angiosperm PRR gene subfamily, illustrating their close relationships with the angiosperm PRRs. However, distinct from the angiosperm sequences, the RLDs of PpPRR2/3/4 exhibit a potential phosphoacceptor aspartic acid-aspartic acid-lysine (DDK) motif. Consistently, the PpPRR2 RID had phosphotransfer ability in vitro, suggesting that PpPRR2 functions as an RR. The PpPRR1 RID, on the other hand, shows a partially diverged DDK motif, and it did not show phosphotransfer ability. All PpPRRs were expressed in a circadian and light-dependent manner, with differential regulation between PpPRR2/4 and PpPRR1/3. Altogether, our results illustrate that PRRs originated from an RR(s) and that there are intraspecific divergences among PpPRRs. Finally, we offer scenarios for the evolution of the PRR family in land plants.
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