Effect of Amino Acid Point Mutations on the Structure and Function of Phytochrome B in Arabidopsis thaliana

doi:10.11983/CBB23074

Abstract

Abstract: Organisms have evolved different photoreceptors to adapt to the ever-changing conditions of the external light environment. Phytochromes (phys) are one of the classic plant photoreceptors, mainly perceiving red and far-red light. Phytochromes detect red and far-red light through the light conversion between the dark-adapted Pr state and the light-activated Pfr state. All plant phytochromes have a conserved N-terminal photoreceptor region and a C-terminal regulatory region. The N-terminal includes NTE, PAS, GAF, and PHY subdomains, while C-terminal includes two PAS domains and a histidine kinase-related domain (HKRD). In order to understand how the structure of photochromes controls its function, many function-deficient photochrome derivatives and amino acid point mutants have been obtained and studied. The N-terminal domain plays important roles in the spectral properties, light signal perception and light signal transduction of phyB. The C-terminal domain is essential for dimerization and nuclear localization of photochrome. This paper mainly reviews point mutations of amino acid in various subdomains of phyB in Arabidopsis thaliana and their effects on the function of phyB, in order to have a better understanding of the structure and functional regulation of phyB. It lays a foundation for obtaining crops with desired agronomic characteristics through gene editing.

Key words: phyB, Arabidopsis thaliana, domain, amino acid point mutation, function

Yanxiao Chen, Yaping Li, Jinjun Zhou, Lixia Xie, Yongbin Peng, Wei Sun, Yanan He, onghui Jiang, Zenglan Wang, Chongke Zheng, Xianzhi Xie. Effect of Amino Acid Point Mutations on the Structure and Function of Phytochrome B in Arabidopsis thaliana[J]. Chinese Bulletin of Botany, 2024, 59(3): 481-494.

Add to citation manager EndNote|Ris|BibTeX

URL: https://www.chinbullbotany.com/EN/10.11983/CBB23074

https://www.chinbullbotany.com/EN/Y2024/V59/I3/481

Figures/Tables 4

References 77

[1]	顾建伟, 刘婧, 薛彦久, 臧新, 谢先芝 (2011). 光敏色素在水稻生长发育中的作用. 中国水稻科学 25, 130-135. DOI
[2]	刘莎, 郑晓明, 冯雳, 乔卫华, 王君瑞, 公婷婷, 梁新霞, 齐兰, 苏龙, 丁膺宾, 许睿, 张丽芳, 程云连, 杨庆文 (2017). 水稻长日抑制基因PhyB的多样性及区域适应性初探. 植物遗传资源学报 18, 283-289. DOI
[3]	童哲, 赵玉锦, 王台, 李念华, 毛居代·亚力 (2000). 植物的光受体和光控发育研究. 植物学报 42, 111-115.
[4]	张芳, 张晓枫, 王进征, 胡勇, 刘祥林 (2011). 植物光敏色素PHYA、PHYB研究进展. 生物学通报 46, 11-14.
[5]	赵翔, 赵青平, 杨煦, 慕世超, 张骁 (2015). 向光素调节植物向光性及其与光敏色素/隐花色素的相互关系. 植物学报 50, 122-132. DOI
[6]	Ádám É, Hussong A, Bindics J, Wüst F, Viczián A, Essing M, Medzihradszky M, Kircher S, Schäfer E, Nagy F (2011). Altered dark- and photo-conversion of phytochrome B mediate extreme light sensitivity and loss of photoreversibility of the phyB-401 mutant. PLoS One 6, e27250.
[7]	Anders K, Daminelli-Widany G, Mroginski MA, von Stetten D, Essen LO (2013). Structure of the cyanobacterial phytochrome 2 photosensor implies a tryptophan switch for phytochrome signaling. J Biol Chem 288, 35714-35725. DOI PMID
[8]	Auldridge ME, Forest KT (2011). Bacterial phytochromes: more than meets the light. Crit Rev Biochem Mol Biol 46, 67-88.
[9]	Bae G, Choi G (2008). Decoding of light signals by plant phytochromes and their interacting proteins. Annu Rev Plant Biol 59, 281-311. DOI PMID
[10]	Bellini D, Papiz MZ (2012). Structure of a bacteriophytochrome and light-stimulated protomer swapping with a gene repressor. Structure 20, 1436-1446. DOI PMID
[11]	Burgie ES, Bussell AN, Walker JM, Dubiel K, Vierstra RD (2014). Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome. Proc Natl Acad Sci USA 111, 10179-10184. DOI PMID
[12]	Burgie ES, Vierstra RD (2014). Phytochromes: an atomic perspective on photoactivation and signaling. Plant Cell 26, 4568-4583.
[13]	Chen D, Lyu M, Kou XX, Li J, Yang ZX, Gao LL, Li Y, Fan LM, Shi H, Zhong SW (2022). Integration of light and temperature sensing by liquid-liquid phase separation of phytochrome B. Mol Cell 82, 3015-3029. DOI PMID
[14]	Chen M, Chory J, Fankhauser C (2004). Light signal transduction in higher plants. Annu Rev Genet 38, 87-117. PMID
[15]	Chen M, Schwab R, Chory J (2003). Characterization of the requirements for localization of phytochrome B to nuclear bodies. Proc Natl Acad Sci USA 100, 14493-14498. PMID
[16]	Chen M, Tao Y, Lim J, Shaw A, Chory J (2005). Regulation of phytochrome B nuclear localization through light-dependent unmasking of nuclear-localization signals. Curr Biol 15, 637-642. DOI PMID
[17]	Cheng MC, Kathare PK, Paik I, Huq E (2021). Phytochrome signaling networks. Annu Rev Plant Biol 72, 217-244.
[18]	Cheng YL, Tu SL (2018). Alternative splicing and cross-talk with light signaling. Plant Cell Physiol 59, 1104-1110.
[19]	Cherry JR, Hondred D, Walker JM, Keller JM, Hershey HP, Vierstra RD (1993). Carboxy-terminal deletion analysis of oat phytochrome A reveals the presence of separate domains required for structure and biological activity. Plant Cell 5, 565-575. DOI PMID
[20]	Cherry JR, Hondred D, Walker JM, Vierstra RD (1992). Phytochrome requires the 6 kDa N-terminal domain for full biological activity. Proc Natl Acad Sci USA 89, 5039-5043. PMID
[21]	Clack T, Mathews S, Sharrock RA (1994). The phytochrome apoprotein family in Arabidopsis is encoded by five genes: the sequences and expression of PHYD and PHYE. Plant Mol Biol 25, 413-427. PMID
[22]	Clack T, Shokry A, Moffet M, Liu P, Faul M, Sharrock RA (2009). Obligate heterodimerization of Arabidopsis phytochromes C and E and interaction with the PIF3 basic helix-loop-helix transcription factor. Plant Cell 21, 786-799. DOI PMID
[23]	Dash L, McEwan RE, Montes C, Mejia L, Walley JW, Dilkes BP, Kelley DR (2021). Slim shady is a novel allele of PHYTOCHROME B present in the T-DNA line SALK_ 015201. Plant Direct 5, e00326.
[24]	Edgerton MD, Jones AM (1992). Localization of protein- protein interactions between subunits of phytochrome. Plant Cell 4, 161-171. PMID
[25]	Elich TD, Chory J (1997). Biochemical characterization of Arabidopsis wild-type and mutant phytochrome B holoproteins. Plant Cell 9, 2271-2280. PMID
[26]	Essen LO, Mailliet J, Hughes J (2008). The structure of a complete phytochrome sensory module in the Pr ground state. Proc Natl Acad Sci USA 105, 14709-14714.
[27]	Franklin KA, Quail PH (2010). Phytochrome functions in Arabidopsis development. J Exp Bot 61, 11-24. DOI PMID
[28]	He YN, Li YP, Cui LX, Xie LX, Zheng CK, Zhou GH, Zhou JJ, Xie XZ (2016). Phytochrome B negatively affects cold tolerance by regulating OsDREB1 gene expression through phytochrome interacting factor-like protein OsPIL16 in rice. Front Plant Sci 7, 1963.
[29]	Hernando CE, Murcia MG, Pereyra ME, Sellaro R, Casal JJ (2021). Phytochrome B links the environment to transcription. J Exp Bot 72, 4068-4084. DOI PMID
[30]	Hu W, Su YS, Lagarias JC (2009). A light-independent allele of phytochrome B faithfully recapitulates photomorphogenic transcriptional networks. Mol Plant 2, 166-182. DOI PMID
[31]	Jung JH, Li Z, Chen H, Yang S, Li DD, Priatama RA, Kumar V, Xuan YH (2023). Mutation of phytochrome B promotes resistance to sheath blight and saline-alkaline stress via increasing ammonium uptake in rice. Plant J 113, 277-290.
[32]	Kikis EA, Oka Y, Hudson ME, Nagatani A, Quail PH (2009). Residues clustered in the light-sensing knot of phytochrome B are necessary for conformer-specific binding to signaling partner PIF3. PLoS Genet 5, e1000352.
[33]	Kim C, Kwon Y, Jeong J, Kang MJ, Lee GS, Moon JH, Lee HJ, Park YI, Choi G (2023). Phytochrome B photobodies are comprised of phytochrome B and its primary and secondary interacting proteins. Nat Commun 14, 1708. DOI PMID
[34]	Kircher S, Gil P, Kozma-Bognár L, Fejes E, Speth V, Husselstein-Muller T, Bauer D, Ádám É, Schäfer E, Nagy F (2002). Nucleocytoplasmic partitioning of the plant photoreceptors phytochrome A, B, C, D, and E is regulated differentially by light and exhibits a diurnal rhythm. Plant Cell 14, 1541-1555. PMID
[35]	Klose C, Venezia F, Hussong A, Kircher S, Schäfer E, Fleck C (2015). Systematic analysis of how phytochrome B dimerization determines its specificity. Nat Plants 1, 15090. DOI PMID
[36]	Krall L, Reed JW (2000). The histidine kinase-related domain participates in phytochrome B function but is dispensable. Proc Natl Acad Sci USA 97, 8169-8174. PMID
[37]	Kretsch T, Poppe C, Schäfer E (2000). A new type of mutation in the plant photoreceptor phytochrome B causes loss of photoreversibility and an extremely enhanced light sensitivity. Plant J 22, 177-186. PMID
[38]	Kwon CT, Song G, Kim SH, Han J, Yoo SC, An G, Kang K, Paek NC (2018). Functional deficiency of phytochrome B improves salt tolerance in rice. Environ Exp Bot 148, 100-108.
[39]	Legris M, Ince YÇ, Fankhauser C (2019). Molecular mechanisms underlying phytochrome-controlled morphogenesis in plants. Nat Commun 10, 5219. DOI PMID
[40]	Li H, Burgie ES, Gannam ZTK, Li HL, Vierstra RD (2022). Plant phytochrome B is an asymmetric dimer with unique signaling potential. Nature 604, 127-133.
[41]	Liu J, Zhang F, Zhou JJ, Chen F, Wang BS, Xie XZ (2012). Phytochrome B control of total leaf area and stomatal density affects drought tolerance in rice. Plant Mol Biol 78, 289-300. DOI PMID
[42]	Liu X, Jiang W, Li YL, Nie HZ, Cui LN, Li RX, Tan L, Peng L, Li C, Luo JY, Li M, Wang HX, Yang J, Zhou B, Wang PC, Liu HT, Zhu JK, Zhao CZ (2023). FERONIA coordinates plant growth and salt tolerance via the phosphorylation of phyB. Nat Plants 9, 645-660. DOI PMID
[43]	Maloof JN, Borevitz JO, Dabi T, Lutes J, Nehring RB, Redfern JL, Trainer GT, Wilson JM, Asami T, Berry CC, Weigel D, Chory J (2001). Natural variation in light sensitivity of Arabidopsis. Nat Genet 29, 441-446. PMID
[44]	Mathews S (2006). Phytochrome-mediated development in land plants: red light sensing evolves to meet the challenges of changing light environments. Mol Ecol 15, 3483-3503. PMID
[45]	Matsushita T, Mochizuki N, Nagatani A (2003). Dimers of the N-terminal domain of phytochrome B are functional in the nucleus. Nature 424, 571-574.
[46]	Medzihradszky M, Bindics J, Ádám É, Viczián A, Klement É, Lorrain S, Gyula P, Mérai Z, Fankhauser C, Medzihradszky KF, Kunkel T, Schäfer E, Nagy F (2013). Phosphorylation of phytochrome B inhibits light-induced signaling via accelerated dark reversion in Arabidopsis. Plant Cell 25, 535-544.
[47]	Nagano S (2016). From photon to signal in phytochromes: similarities and differences between prokaryotic and plant phytochromes. J Plant Res 129, 123-135. DOI PMID
[48]	Nito K, Wong CCL, Yates III JR, Chory J (2013). Tyrosine phosphorylation regulates the activity of phytochrome photoreceptors. Cell Rep 3, 1970-1979. DOI PMID
[49]	Oka Y, Matsushita T, Mochizuki N, Quail PH, Nagatani A (2008). Mutant screen distinguishes between residues necessary for light-signal perception and signal transfer by phytochrome B. PLoS Genet 4, e1000158.
[50]	Oka Y, Matsushita T, Mochizuki N, Suzuki T, Tokutomi S, Nagatani A (2004). Functional analysis of a 450-amino acid N-terminal fragment of phytochrome B in Arabidopsis. Plant Cell 16, 2104-2116.
[51]	Paik I, Huq E (2019). Plant photoreceptors: multi-functional sensory proteins and their signaling networks. Semin Cell Dev Biol 92, 114-121. DOI PMID
[52]	Qiu YJ, Pasoreck EK, Reddy AK, Nagatani A, Ma WX, Chory J, Chen M (2017). Mechanism of early light signaling by the carboxy-terminal output module of Arabidopsis phytochrome B. Nat Commun 8, 1905.
[53]	Quail PH (2002). Phytochrome photosensory signaling networks. Nat Rev Mol Cell Biol 3, 85-93.
[54]	Reed JW, Nagpal P, Poole DS, Furuya M, Chory J (1993). Mutations in the gene for the red/far-red light receptor phytochrome B alter cell elongation and physiological responses throughout Arabidopsis development. Plant Cell 5, 147-157. PMID
[55]	Rockwell NC, Lagarias JC (2006). The structure of phytochrome: a picture is worth a thousand spectra. Plant Cell 18, 4-14. DOI PMID
[56]	Rockwell NC, Su YS, Lagarias JC (2006). Phytochrome structure and signaling mechanisms. Annu Rev Plant Biol 57, 837-858. PMID
[57]	Ruiz-Diaz MJ, Matsusaka D, Cascales J, Sánchez DH, Sánchez-Lamas M, Cerdán PD, Botto JF (2022). Functional analysis of PHYB polymorphisms in Arabidopsis thaliana collected in Patagonia. Front Plant Sci 13, 952214.
[58]	Sharrock RA, Quail PH (1989). Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family. Genes Dev 3, 1745-1757.
[59]	Su YS, Lagarias JC (2007). Light-independent phytochrome signaling mediated by dominant GAF domain tyrosine mutants of Arabidopsis phytochromes in transgenic plants. Plant Cell 19, 2124-2139.
[60]	Sun W, Xu XH, Lu XB, Xie LX, Bai B, Zheng CK, Sun HW, He YN, Xie XZ (2017). The rice phytochrome genes, PHYA and PHYB, have synergistic effects on anther development and pollen viability. Sci Rep 7, 6439.
[61]	Velázquez Escobar F, Buhrke D, Fernandez Lopez M, Shenkutie SM, von Horsten S, Essen LO, Hughes J, Hildebrandt P (2017). Structural communication between the chromophore-binding pocket and the N-terminal extension in plant phytochrome phyB. FEBS Lett 591, 1258-1265. DOI PMID
[62]	Viczián A, Ádám É, Staudt AM, Lambert D, Klement E, Romero Montepaone S, Hiltbrunner A, Casal J, Schäfer E, Nagy F, Klose C (2020). Differential phosphorylation of the N-terminal extension regulates phytochrome B signaling. New Phytol 225, 1635-1650. DOI PMID
[63]	Viczián A, Nagy F (2024). Phytochrome B phosphorylation expanded: site-specific kinases are identified. New Phytol 241, 65-72.
[64]	Vierstra RD (1993). Illuminating phytochrome functions (There is light at the end of the tunnel). Plant Physiol 103, 679-684. PMID
[65]	Wagner D, Koloszvari M, Quail PH (1996). Two small spatially distinct regions of phytochrome B are required for efficient signaling rates. Plant Cell 8, 859-871.
[66]	Wagner D, Quail PH (1995). Mutational analysis of phytochrome B identifies a small COOH-terminal-domain region critical for regulatory activity. Proc Natl Acad Sci USA 92, 8596-8600. PMID
[67]	Wagner JR, Brunzelle JS, Forest KT, Vierstra RD (2005). A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome. Nature 438, 325-331.
[68]	Wagner JR, Zhang JR, Brunzelle JS, Vierstra RD, Forest KT (2007). High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution. J Biol Chem 282, 12298-12309.
[69]	Wies G, Mantese AI, Casal JJ, Maddonni GÁ (2019). Phytochrome B enhances plant growth, biomass and grain yield in field-grown maize. Ann Bot 123, 1079-1088.
[70]	Xie XZ, Shinomura T, Inagaki N, Kiyota S, Takano M (2007). Phytochrome-mediated inhibition of coleoptile growth in rice: age-dependency and action spectra. Photochem Photobiol 83, 131-138. PMID
[71]	Xie XZ, Xue YJ, Zhou JJ, Zhang B, Chang H, Takano M (2011). Phytochromes regulate SA and JA signaling pathways in rice and are required for developmentally controlled resistance to Magnaporthe grisea. Mol Plant 4, 688-696.
[72]	Xu Y, Parks BM, Short TW, Quail PH (1995). Missense mutations define a restricted segment in the C-terminal domain of phytochrome A critical to its regulatory activity. Plant Cell 7, 1433-1443. PMID
[73]	Yamaguchi R, Nakamura M, Mochizuki N, Kay SA, Nagatani A (1999). Light-dependent translocation of a phytochrome B-GFP fusion protein to the nucleus in transgenic Arabidopsis. J Cell Biol 145, 437-445. DOI PMID
[74]	Yang XJ, Kuk J, Moffat K (2008). Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction. Proc Natl Acad Sci USA 105, 14715-14720.
[75]	Yang XJ, Kuk J, Moffat K (2009). Conformational differences between the Pfr and Pr states in Pseudomonas aeruginosa bacteriophytochrome. Proc Natl Acad Sci USA 106, 15639-15644.
[76]	Zhang JR, Stankey RJ, Vierstra RD (2013). Structure- guided engineering of plant phytochrome B with altered photochemistry and light signaling. Plant Physiol 161, 1445-1457.
[77]	Zhao Y, Shi H, Pan Y, Lyu M, Yang ZX, Kou XX, Deng XW, Zhong SW (2023). Sensory circuitry controls cytosolic calcium-mediated phytochrome B phototransduction. Cell 186, 1230-1243. DOI PMID

结构域	突变位点	光敏感性	发色团组装及结合	光敏色素稳定性	光小体形成	光敏色素核定位	光信号传递	参考文献
NTE	D64N	-						Oka et al., 2008
	S80A					-		Zhao et al., 2023
	S86D(A)	-(+)		o(o)			-	Medzihradszky et al., 2013; Viczián et al., 2020
PAS	Y104E	-					-	Nito et al., 2013
	S106A					-	-	Zhao et al., 2023
	R110Q	-					-	Oka et al., 2008; Kikis et al., 2009
	G111D	-					-	Oka et al., 2008; Kikis et al., 2009
	G112D	-					-	Oka et al., 2008
	G118R		-					Oka et al., 2008
	C119Y		-				-	Kikis et al., 2009
	S134G	-	-				-	Oka et al., 2008; Kikis et al., 2009
	I143L	+						Ruiz-Diaz et al., 2022
PAS	P149L	-						Oka et al., 2008
PAS	I208T	-	o					Oka et al., 2008
	S227A			+			-	Liu et al., 2023
GAF	L256C		-					Kikis et al., 2009
	V264E		-					Kikis et al., 2009
	V273L		-					Kikis et al., 2009
	Y276H	+					+	Su and Lagarias, 2007; Bae and Choi, 2008; Hu et al., 2009
	H283T			-				Reed et al., 1993; Oka et al., 2008
	G284E	-						Oka et al., 2008
	P304L	o		o			-	Oka et al., 2008
	I308T		o					Kikis et al., 2009
	P309L	-						Oka et al., 2008
	R313K	-	o	-				Oka et al., 2008
	R322Q	-	o	-				Oka et al., 2008
	C327Y			-				Chen et al., 2003; Oka et al., 2008
	S343Y		-					Kikis et al., 2009
	C345R		-					Kikis et al., 2009
	R352K	o		o			-	Oka et al., 2008
	C357S		-					Wagner et al., 1996
	S367P		o					Kikis et al., 2009
	S370F	-						Oka et al., 2008
	A372T	-		-				Chen et al., 2003; Oka et al., 2008
	V401I	-	o	-				Oka et al., 2008
	P411L		-					Kikis et al., 2009
	R415W		-					Kikis et al., 2009
PHY	D453R	+		+				Viczian et al., 2020
	G564E(A)	+	o	+			+(-)	Kretsch et al., 2000; Oka et al., 2008
	M579T	-						Maloof et al., 2001; Burgie et al., 2014
	R582A	+		+				Burgie et al., 2014
	S584F			-				Oka et al., 2008
	A587T			-		-		Chen et al., 2003; Oka et al., 2008
PRD	G674D	-			-			Chen et al., 2003
	A719V	-			-			Chen et al., 2003
	A750V	-					-	Wagner and Quail, 1995
	G767E(R)	-(-)					-(-)	Wagner and Quail, 1995; Matsushita et al., 2003
	E812K	-		-			-	Wagner and Quail, 1995; Elich and Chory, 1997; Chen et al., 2003
HKRD	V980I	-						Ruiz-Diaz et al., 2022
	D1040V	-			-		-	Qiu et al., 2017; Kwon et al., 2018
	L1072V	-						Ruiz-Diaz et al., 2022

结构域	突变位点	光敏感性	发色团组装及结合	光敏色素稳定性	光小体形成	光敏色素核定位	光信号传递	参考文献
NTE	D64N	-						Oka et al., 2008
	S80A					-		Zhao et al., 2023
	S86D(A)	-(+)		o(o)			-	Medzihradszky et al., 2013; Viczián et al., 2020
PAS	Y104E	-					-	Nito et al., 2013
	S106A					-	-	Zhao et al., 2023
	R110Q	-					-	Oka et al., 2008; Kikis et al., 2009
	G111D	-					-	Oka et al., 2008; Kikis et al., 2009
	G112D	-					-	Oka et al., 2008
	G118R		-					Oka et al., 2008
	C119Y		-				-	Kikis et al., 2009
	S134G	-	-				-	Oka et al., 2008; Kikis et al., 2009
	I143L	+						Ruiz-Diaz et al., 2022
PAS	P149L	-						Oka et al., 2008
PAS	I208T	-	o					Oka et al., 2008
	S227A			+			-	Liu et al., 2023
GAF	L256C		-					Kikis et al., 2009
	V264E		-					Kikis et al., 2009
	V273L		-					Kikis et al., 2009
	Y276H	+					+	Su and Lagarias, 2007; Bae and Choi, 2008; Hu et al., 2009
	H283T			-				Reed et al., 1993; Oka et al., 2008
	G284E	-						Oka et al., 2008
	P304L	o		o			-	Oka et al., 2008
	I308T		o					Kikis et al., 2009
	P309L	-						Oka et al., 2008
	R313K	-	o	-				Oka et al., 2008
	R322Q	-	o	-				Oka et al., 2008
	C327Y			-				Chen et al., 2003; Oka et al., 2008
	S343Y		-					Kikis et al., 2009
	C345R		-					Kikis et al., 2009
	R352K	o		o			-	Oka et al., 2008
	C357S		-					Wagner et al., 1996
	S367P		o					Kikis et al., 2009
	S370F	-						Oka et al., 2008
	A372T	-		-				Chen et al., 2003; Oka et al., 2008
	V401I	-	o	-				Oka et al., 2008
	P411L		-					Kikis et al., 2009
	R415W		-					Kikis et al., 2009
PHY	D453R	+		+				Viczian et al., 2020
	G564E(A)	+	o	+			+(-)	Kretsch et al., 2000; Oka et al., 2008
	M579T	-						Maloof et al., 2001; Burgie et al., 2014
	R582A	+		+				Burgie et al., 2014
	S584F			-				Oka et al., 2008
	A587T			-		-		Chen et al., 2003; Oka et al., 2008
PRD	G674D	-			-			Chen et al., 2003
	A719V	-			-			Chen et al., 2003
	A750V	-					-	Wagner and Quail, 1995
	G767E(R)	-(-)					-(-)	Wagner and Quail, 1995; Matsushita et al., 2003
	E812K	-		-			-	Wagner and Quail, 1995; Elich and Chory, 1997; Chen et al., 2003
HKRD	V980I	-						Ruiz-Diaz et al., 2022
	D1040V	-			-		-	Qiu et al., 2017; Kwon et al., 2018
	L1072V	-						Ruiz-Diaz et al., 2022

模块	亚结构域	功能	主要作用
PSM	NTE	调控光敏色素Pfr形式的稳定性, 如影响光敏色素的热逆转反应; 负责光信号传递, 如影响phyB与下游转录因子PIF结合及通过光-钙调控环促进phyB入核	光信号感知及传递
	PAS	调控发色团的组装; 负责光信号传递, 如影响phyB与下游转录因子PIF3的结合能力
	GAF	负责发色团的组装, 感应光信号; 维持phyB Pr/Pfr形式正常的可逆转换; 保持光敏色素Pfr形式的数量或整体结构, 如影响phyB的暗逆转率; 负责光信号传递, 如感光结可能直接与PIF相互作用
	PHY	调控光敏色素Pfr形式的稳定性, 如影响phyB的暗逆转率以及热逆转反应; 维持phyB Pr/Pfr形式正常的可逆转换; 负责光信号传递, 如影响phyB与下游成分的相互作用及phyB的核定位
OPM	PRD	调控光敏色素Pfr形式的稳定性, 如影响phyB的暗逆转反应; 负责光信号传递, 如影响phyB的核定位	光信号传递
OPM	HKRD	介导光敏色素的二聚化, 从而影响phyB在核内积累和光小体定位中的早期信号传递	光信号传递

模块	亚结构域	功能	主要作用
PSM	NTE	调控光敏色素Pfr形式的稳定性, 如影响光敏色素的热逆转反应; 负责光信号传递, 如影响phyB与下游转录因子PIF结合及通过光-钙调控环促进phyB入核	光信号感知及传递
	PAS	调控发色团的组装; 负责光信号传递, 如影响phyB与下游转录因子PIF3的结合能力
	GAF	负责发色团的组装, 感应光信号; 维持phyB Pr/Pfr形式正常的可逆转换; 保持光敏色素Pfr形式的数量或整体结构, 如影响phyB的暗逆转率; 负责光信号传递, 如感光结可能直接与PIF相互作用
	PHY	调控光敏色素Pfr形式的稳定性, 如影响phyB的暗逆转率以及热逆转反应; 维持phyB Pr/Pfr形式正常的可逆转换; 负责光信号传递, 如影响phyB与下游成分的相互作用及phyB的核定位
OPM	PRD	调控光敏色素Pfr形式的稳定性, 如影响phyB的暗逆转反应; 负责光信号传递, 如影响phyB的核定位	光信号传递
OPM	HKRD	介导光敏色素的二聚化, 从而影响phyB在核内积累和光小体定位中的早期信号传递	光信号传递