Photosensing and Thermosensing by Phytochrome B Require Both Proximal and Distal Allosteric Features within the Dimeric Photoreceptor

Burgie, E. Sethe; Bussell, Adam N.; Lye, Shu-Hui; Wang, Tong; Hu, Weiming; McLoughlin, Katrice E.; Weber, Erin L.; Li, Huilin; Vierstra, Richard D.

doi:10.1038/s41598-017-14037-0

Photosensing and Thermosensing by Phytochrome B Require Both Proximal and Distal Allosteric Features within the Dimeric Photoreceptor

Journal Article · Fri Oct 20 00:00:00 EDT 2017 · Scientific Reports

DOI:https://doi.org/10.1038/s41598-017-14037-0· OSTI ID:1624353

Burgie, E. Sethe ^[1]; Bussell, Adam N. ^[2]; Lye, Shu-Hui ^[3]; Wang, Tong ^[4]; Hu, Weiming ^[5]; McLoughlin, Katrice E. ^[5]; Weber, Erin L. ^[2]; Li, Huilin ^[6]; Vierstra, Richard D. ^[3]

Washington Univ., St. Louis, MO (United States). Dept. of Biology; Univ. of Wisconsin, Madison, WI (United States). Dept. of Genetics; DOE/OSTI
Univ. of Wisconsin, Madison, WI (United States). Dept. of Genetics
Washington Univ., St. Louis, MO (United States). Dept. of Biology; Univ. of Wisconsin, Madison, WI (United States). Dept. of Genetics
Brookhaven National Lab. (BNL), Upton, NY (United States). Dept. of Biology; City Univ. of New York (CUNY), NY (United States). CUNY Advanced Science Research Center
Washington Univ., St. Louis, MO (United States). Dept. of Biology
Brookhaven National Lab. (BNL), Upton, NY (United States). Dept. of Biology; Van Andel Research Inst. (VARI), Grand Rapids, MI (United States)

Phytochromes (Phys) encompass a diverse collection of bilin-containing photoreceptors that help plants and microorganisms perceive light through photointerconversion between red light (Pr) and far-red light (Pfr)-absorbing states. In addition, Pfr reverts thermally back to Pr via a highly enthalpic process that enables temperature sensation in plants and possibly other organisms. Through domain analysis of the Arabidopsis PhyB isoform assembled recombinantly, coupled with measurements of solution size, photoconversion, and thermal reversion, we identified both proximal and distal features that influence all three metrics. Included are the downstream C-terminal histidine kinase-related domain known to promote dimerization and a conserved patch just upstream of an N-terminal Period/Arnt/Sim (PAS) domain, which upon removal dramatically accelerates thermal reversion. We also discovered that the nature of the bilin strongly influences Pfr stability. Whereas incorporation of the native bilin phytochromobilin into PhyB confers robust Pfr → Pr thermal reversion, that assembled with the cyanobacterial version phycocyanobilin, often used for optogenetics, has a dramatically stabilized Pfr state. Taken together, we conclude that Pfr acquisition and stability are impacted by a collection of opposing allosteric features that inhibit or promote photoconversion and reversion of Pfr back to Pr, thus allowing Phys to dynamically measure light, temperature, and possibly time.

View Accepted Manuscript (DOE)

Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: National Institute of Health; National Science Foundation; USDOE Office of Science (SC)

Grant/Contract Number:: SC0012704

OSTI ID:: 1624353

Journal Information:: Scientific Reports, Journal Name: Scientific Reports Journal Issue: 1 Vol. 7; ISSN 2045-2322

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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