International Prize for Biology
25th Recipient (2009)
The Committee on the International Prize for Biology of Japan Society
for the Promotion of Science awards the 2009 International Prize for Biology
in the field of "Biology of Sensing" to
Dr. Winslow Russell BRIGGS, Director Emeritus, Carnegie Institution of Washington, U.S.A.
for the Promotion of Science awards the 2009 International Prize for Biology
in the field of "Biology of Sensing" to
Dr. Winslow Russell BRIGGS, Director Emeritus, Carnegie Institution of Washington, U.S.A.
On Tuesday, September 15, 2009, at a meeting of the Committee on the International Prize for Biology (chaired by Dr. Takashi Sugimura, Secretary General, The Japan Academy) of the Japan Society for the Promotion of Science decided to present the 25th (2009) International Prize for Biology to Dr. Winslow Russell Briggs, an American citizen who is Director Emeritus, Department of Plant Biology, Carnegie Institution of Washington, USA, and Professor Emeritus, Department of Biological Sciences, Stanford University, USA. The field of specialization for the 25th Prize is "Biology of Sensing."
Dr. Winslow Russell BRIGGS
DATE OF BIRTH : April 29, 1928
CITIZENSHIP : United States of America
POSITION : Director Emeritus, Department of Plant Biology, Carnegie Institution of Washington, USA, Professor Emeritus, Department of Biological Sciences, Stanford University, USA
The Selection Committee, established by the Committee on the International Prize for Biology and chaired by Makoto Asashima, Director of Development Research Laboratory, AIST, distributed a total of 1,890 recommendation forms to Japanese and foreign universities, research centers, academic associations, individual researchers, and international academic organizations involved in the subject field of biology, and received a total of 57 recommendations in response. As some of these recommendations named the same individuals, the actual number of individuals recommended was 46, from 16 countries. The Selection Committee met a total of four times and very carefully reviewed all the candidates. Ultimately, the Committee decided to recommend Dr. Winslow Russell Briggs as the recipient of the 25th International Prize for Biology.
Over a research career spanning more than fifty years, Dr. Briggs has consistently focused on the photoresponse mechanism by which plants respond to light information, their principal means of detecting seasonal changes and environmental conditions. In particular, he has made a series of breakthroughs concerning phototropism, a topic of intense interest to plant scientists since Charles Darwin first investigated the phenomenon. The highly original work that led Dr. Briggs to discover phototropins—blue-light-activated proteins that serve as directional photoreceptors for phototropism—has contributed greatly to the study of photoresponses in organisms from bacteria to the higher plants. As light receptors involved not only in phototropism, but also in stomatal opening, chloroplast movement, and other vital functions, phototropins have proved to be very important to plant survival.
Dr. Briggs has characterized the basic molecular properties of phototropins, showing that the N-terminal end of the protein contains two sites, known as LOV domains, each of which binds a molecule of light-absorbing flavin mononucleotide (FMN), while the C-terminal end has a kinase function. The LOV domain sequences, consisting of about 110 amino acids, have been found to be highly conserved between species ranging from bacteria to spermatophytes; based on these sequences, many more blue-light receptors with different functional sites have been discovered in a diverse group of organisms including bacteria, fungi, algae, mosses, and ferns. Also, the recent discovery by Dr. Briggs and his colleagues that Brucella abortus, a bacterium that causes infectious disease in livestock and humans, becomes more virulent on exposure to blue light has revealed that light contributes to the process of bacterial infection in animals, including humans.
Dr. Briggs’s discovery of phototropins and their LOV domains has thus greatly enhanced our understanding of the utilization of light, not only in plants but in all living things, and major benefits stand to be gained as the resulting knowledge is put to use. The enormous value of this contribution, to biological science as a whole and to society at large, makes Dr. Briggs a worthy recipient of the International Prize for Biology.
Dr. Briggs has characterized the basic molecular properties of phototropins, showing that the N-terminal end of the protein contains two sites, known as LOV domains, each of which binds a molecule of light-absorbing flavin mononucleotide (FMN), while the C-terminal end has a kinase function. The LOV domain sequences, consisting of about 110 amino acids, have been found to be highly conserved between species ranging from bacteria to spermatophytes; based on these sequences, many more blue-light receptors with different functional sites have been discovered in a diverse group of organisms including bacteria, fungi, algae, mosses, and ferns. Also, the recent discovery by Dr. Briggs and his colleagues that Brucella abortus, a bacterium that causes infectious disease in livestock and humans, becomes more virulent on exposure to blue light has revealed that light contributes to the process of bacterial infection in animals, including humans.
Dr. Briggs’s discovery of phototropins and their LOV domains has thus greatly enhanced our understanding of the utilization of light, not only in plants but in all living things, and major benefits stand to be gained as the resulting knowledge is put to use. The enormous value of this contribution, to biological science as a whole and to society at large, makes Dr. Briggs a worthy recipient of the International Prize for Biology.
The award ceremony will be held on Monday, November 30, 2009, at the Japan Academy (7-32 Ueno Koen, Taito-ku, Tokyo). Each year, Their Majesties the Emperor and Empress attend the ceremony and a party in honor of the award recipient.
To commemorate the award to Dr. Winslow Russell Briggs, the 25th International Prize for Biology Commemorative Symposium on Genetics will take place on Wednesday, December 2 and Thursday, December 3, 2009, at Kyoto University
To commemorate the award to Dr. Winslow Russell Briggs, the 25th International Prize for Biology Commemorative Symposium on Genetics will take place on Wednesday, December 2 and Thursday, December 3, 2009, at Kyoto University
1974 Elected to National Academy of Sciences
1975 Elected to American Academy of Arts and Sciences
1984 – 1985 Alexander von Humboldt U.S. Senior Scientist Award
1986 Elected to Deutsche Akademie der Naturforscher Leopoldina
1993 – 1994 Alexander von Humboldt U. S. Senior Scientist Award
1994 Stephen Hales Prize, American Society of Plant Physiologists
1995 Sterling Hendricks Medal, United States Department of Agriculture and American Chemical Society
2000 Finsen Medal, Association Internationale de Photobiologie
2006 Centennial Award, Botanical Society of America
2007 Gude Prize, American Society of Plant Biologists
1975 Elected to American Academy of Arts and Sciences
1984 – 1985 Alexander von Humboldt U.S. Senior Scientist Award
1986 Elected to Deutsche Akademie der Naturforscher Leopoldina
1993 – 1994 Alexander von Humboldt U. S. Senior Scientist Award
1994 Stephen Hales Prize, American Society of Plant Physiologists
1995 Sterling Hendricks Medal, United States Department of Agriculture and American Chemical Society
2000 Finsen Medal, Association Internationale de Photobiologie
2006 Centennial Award, Botanical Society of America
2007 Gude Prize, American Society of Plant Biologists
No less today, at the age of 81, than when he embarked on his career as a plant scientist, Dr. Briggs’s interest has consistently focused on how plants utilize light information and on the photoreceptors and the signaling mechanisms involved.
Charles Darwin and his son Francis were among the first to study phototropism, the phenomenon in which plants bend in the direction of light. Using young coleoptiles of monocotyledons, they determined that light is detected at the tip and a signal of some kind then travels to the lower part of the coleoptile, where it induces bending. Since Darwin’s time, phototropism has remained a central problem in plant physiology.
Among Dr. Briggs’s many outstanding achievements in his work on light information, he has made a number of especially important breakthroughs in this area. In particular, his discovery of the photoreceptors that mediate phototropism has led to a major rethinking of how light is utilized by many organisms, from spermatophytes to bacteria.
1) Lateral Movement of Auxin
In 1926, Frits Went discovered growth-accelerating substances, which he named auxins, that move from the tip of the coleoptile toward the base. In what has become known as the Cholodny-Went theory (1926), he suggested that in a coleoptile illuminated from one side, phototropic curvature is induced by a difference in auxin concentration between the lighted and dark sides. The cause of such an auxin differential was unclear, however; among the possibilities suggested were light dependence of auxin synthesis, or of the rate of auxin breakdown, or of the activity level of an inhibitor. In 1957, Dr. Briggs settled this debate by inserting a partial or complete barrier (a thin cover glass) between the illuminated and dark sides of coleoptiles and measuring the amount of auxin recovered from their bases, thereby demonstrating that neither the synthesis nor the breakdown of auxin was influenced by the presence or direction of light; instead, a concentration differential developed as auxin moved from the lighted to the shaded side in the tissue of the coleoptile tip.
2) Light Sensitivity in Phototropism
Phototropism in higher plants is induced by blue light. Red light was therefore used as the traditional “safelight” for experimental manipulation and observation of phototropism, as it was thought not to influence the response. However, Dr. Briggs discovered that supposedly “safe” red light induced a phytochrome-mediated alteration in phototropic sensitivity to blue light (1966). He subsequently found that red light treatments in the very low fluence range regulated the elongation growth of etiolated seedlings and the gene expression of proteins necessary for chloroplast development, effects that he called “very low-irradiance response” (1981), and he proposed dim green light as the laboratory safelight for phytochrome work. He also showed that the tissues of etiolated seedlings act like fiber optics, piping light down through the soil to the root (1982). Since this work, researchers have handled experimental manipulations of phototropism with extreme care.
3) The Discovery of Phototropins
Identifying the photoreceptors involved in phototropism remained a challenge for many years, not only in the higher plants but also in cryptogams such as the fungus Phycomyces. Around 1990, Dr. Briggs adopted a two-pronged approach: biochemical investigation of a protein that is phosphorylated by blue light irradiation, and genetic studies using non-phototropic mutants of Arabidopsis (thale cress). The discovery of a plasma membrane-associated protein that becomes phosphorylated upon irradiation with blue light (1988) led to identification of the photoreceptors that mediate phototropism. In 1997, Dr. Briggs isolated the causative gene (NPH1) of the variant nph1 (non-phototropic hypocotyl 1) in Arabidopsis; in 1998, he determined that this gene encodes the photoreceptors, and in 1999 he named them phototropins. At the amino-terminal (N-terminal) end, these photoreceptor proteins were found to contain two LOV domains, LOV1 and LOV2; these are sequences of about 110 amino acids that share homology with a group of sensor proteins regulated by light, oxygen, or voltage (hence the term “LOV domain”), and that act as a light sensor in this case. The carboxyl-terminal (C-terminal) end was found to have a kinase structure, making it the functional portion of the protein. In quick succession, Dr. Briggs determined the basic molecular properties of phototropin: each LOV domain binds a molecule of the chromophore flavin mononucleotide (FMN) at a conserved cysteine residue (1998); the protein undergoes autophosphorylation on absorbing light (1998); it is activated when a temporary covalent bond is formed between the cysteine residue and FMN within the LOV domain (2000); and the light-activated LOV domain reverts in darkness to its initial ground state (2000). Dr. Briggs’s work has also clarified a number of phenomena thought to underlie the physiological response, indicating, for example, that of the two LOV domains, only LOV2 is essential to light sensing (2002); that phototropin 1 is localized to the plasma membrane under dark conditions, but becomes released to the cytoplasm in response to light (2002); and that this intracellular redistribution is inhibited by pretreatment with brief pulses of red light, an effect that is implicated in changes in phototropic sensitivity (2008).
4) Consequences of the Discovery of Phototropins
Progress in the genome analysis of various species has led to the discovery of LOV domains—the light-sensing regions of phototropins—in prokaryotic organisms such as bacteria and cyanobacteria, and has also shown that the domains are conserved in many non-animal eukaryotes, such as fungi, algae, mosses, and ferns. As a result, in a number of different species with blue light responses whose physiology had been well studied, the blue-light receptors are now being identified for the first time. Surprisingly, they are turning out to consist of novel photoreceptor proteins in which the LOV domains are coupled to functional domains quite distinct from those of phototropin. These findings mean that, in evolutionary processes, many organisms have deployed LOV domains as effective light switches to control physiologically active proteins by means of light. LOV photoreceptors are now being discovered even in bacteria, which were previously thought to be little influenced by light. Dr. Briggs and his colleagues have recently shown that in Brucella abortus, a bacterium that causes an infectious disease in livestock, the infection process involves light activation of LOV photoreceptor proteins, and have suggested that the role of light also needs to be considered in disease transmission in mammals (2007).
Thus, the significance of Dr. Briggs’s discovery of phototropin extends far beyond the identification of a single blue-light photoreceptor to encompass the characterization of LOV domains that are widespread among living things, and his work has been a great seminal influence in the field of photobiology.
Charles Darwin and his son Francis were among the first to study phototropism, the phenomenon in which plants bend in the direction of light. Using young coleoptiles of monocotyledons, they determined that light is detected at the tip and a signal of some kind then travels to the lower part of the coleoptile, where it induces bending. Since Darwin’s time, phototropism has remained a central problem in plant physiology.
Among Dr. Briggs’s many outstanding achievements in his work on light information, he has made a number of especially important breakthroughs in this area. In particular, his discovery of the photoreceptors that mediate phototropism has led to a major rethinking of how light is utilized by many organisms, from spermatophytes to bacteria.
1) Lateral Movement of Auxin
In 1926, Frits Went discovered growth-accelerating substances, which he named auxins, that move from the tip of the coleoptile toward the base. In what has become known as the Cholodny-Went theory (1926), he suggested that in a coleoptile illuminated from one side, phototropic curvature is induced by a difference in auxin concentration between the lighted and dark sides. The cause of such an auxin differential was unclear, however; among the possibilities suggested were light dependence of auxin synthesis, or of the rate of auxin breakdown, or of the activity level of an inhibitor. In 1957, Dr. Briggs settled this debate by inserting a partial or complete barrier (a thin cover glass) between the illuminated and dark sides of coleoptiles and measuring the amount of auxin recovered from their bases, thereby demonstrating that neither the synthesis nor the breakdown of auxin was influenced by the presence or direction of light; instead, a concentration differential developed as auxin moved from the lighted to the shaded side in the tissue of the coleoptile tip.
2) Light Sensitivity in Phototropism
Phototropism in higher plants is induced by blue light. Red light was therefore used as the traditional “safelight” for experimental manipulation and observation of phototropism, as it was thought not to influence the response. However, Dr. Briggs discovered that supposedly “safe” red light induced a phytochrome-mediated alteration in phototropic sensitivity to blue light (1966). He subsequently found that red light treatments in the very low fluence range regulated the elongation growth of etiolated seedlings and the gene expression of proteins necessary for chloroplast development, effects that he called “very low-irradiance response” (1981), and he proposed dim green light as the laboratory safelight for phytochrome work. He also showed that the tissues of etiolated seedlings act like fiber optics, piping light down through the soil to the root (1982). Since this work, researchers have handled experimental manipulations of phototropism with extreme care.
3) The Discovery of Phototropins
Identifying the photoreceptors involved in phototropism remained a challenge for many years, not only in the higher plants but also in cryptogams such as the fungus Phycomyces. Around 1990, Dr. Briggs adopted a two-pronged approach: biochemical investigation of a protein that is phosphorylated by blue light irradiation, and genetic studies using non-phototropic mutants of Arabidopsis (thale cress). The discovery of a plasma membrane-associated protein that becomes phosphorylated upon irradiation with blue light (1988) led to identification of the photoreceptors that mediate phototropism. In 1997, Dr. Briggs isolated the causative gene (NPH1) of the variant nph1 (non-phototropic hypocotyl 1) in Arabidopsis; in 1998, he determined that this gene encodes the photoreceptors, and in 1999 he named them phototropins. At the amino-terminal (N-terminal) end, these photoreceptor proteins were found to contain two LOV domains, LOV1 and LOV2; these are sequences of about 110 amino acids that share homology with a group of sensor proteins regulated by light, oxygen, or voltage (hence the term “LOV domain”), and that act as a light sensor in this case. The carboxyl-terminal (C-terminal) end was found to have a kinase structure, making it the functional portion of the protein. In quick succession, Dr. Briggs determined the basic molecular properties of phototropin: each LOV domain binds a molecule of the chromophore flavin mononucleotide (FMN) at a conserved cysteine residue (1998); the protein undergoes autophosphorylation on absorbing light (1998); it is activated when a temporary covalent bond is formed between the cysteine residue and FMN within the LOV domain (2000); and the light-activated LOV domain reverts in darkness to its initial ground state (2000). Dr. Briggs’s work has also clarified a number of phenomena thought to underlie the physiological response, indicating, for example, that of the two LOV domains, only LOV2 is essential to light sensing (2002); that phototropin 1 is localized to the plasma membrane under dark conditions, but becomes released to the cytoplasm in response to light (2002); and that this intracellular redistribution is inhibited by pretreatment with brief pulses of red light, an effect that is implicated in changes in phototropic sensitivity (2008).
4) Consequences of the Discovery of Phototropins
Progress in the genome analysis of various species has led to the discovery of LOV domains—the light-sensing regions of phototropins—in prokaryotic organisms such as bacteria and cyanobacteria, and has also shown that the domains are conserved in many non-animal eukaryotes, such as fungi, algae, mosses, and ferns. As a result, in a number of different species with blue light responses whose physiology had been well studied, the blue-light receptors are now being identified for the first time. Surprisingly, they are turning out to consist of novel photoreceptor proteins in which the LOV domains are coupled to functional domains quite distinct from those of phototropin. These findings mean that, in evolutionary processes, many organisms have deployed LOV domains as effective light switches to control physiologically active proteins by means of light. LOV photoreceptors are now being discovered even in bacteria, which were previously thought to be little influenced by light. Dr. Briggs and his colleagues have recently shown that in Brucella abortus, a bacterium that causes an infectious disease in livestock, the infection process involves light activation of LOV photoreceptor proteins, and have suggested that the role of light also needs to be considered in disease transmission in mammals (2007).
Thus, the significance of Dr. Briggs’s discovery of phototropin extends far beyond the identification of a single blue-light photoreceptor to encompass the characterization of LOV domains that are widespread among living things, and his work has been a great seminal influence in the field of photobiology.
- Briggs, W. R., R. D. Tocher, and J. F. Wilson. 1957. Phototropic auxin redistribution in corn coleoptiles. Science 126:210-212.
- Briggs, W. R. 1963. The phototropic responses of higher plants. Ann. Rev. Plant Physiol. 14:311-352.
- Pratt, L. H. and W. R. Briggs. 1966. Photochemical and nonphotochemical reactions of phytochrome in vivo. Plant Physiol. 41: 467-474.
- Briggs, W. R. and H. P. Chon. 1966. The physiological versus the spectrophotometric status of phytochrome in corn coleoptiles. Plant Physiol. 41:1159-1166.
- Sargent, M. L. and W. R. Briggs. 1967. The effects of light on a circadian rhythm of conidiation in Neurospora. Plant Physiol. 42:1504-1510.
- Briggs, W. R. and D. C. Fork. 1969. Long-lived intermediates in phytochrome transformation I: In vitro studies. Plant Physiol. 44:1081-1088.
- Gardner, G., C. S. Pike, H. V. Rice, and W. R. Briggs. 1971. "Disaggregation" of phytochrome in vitro - a consequence of proteolysis. Plant Physiol. 48:686-693.
- Briggs, W. R. and H. V. Rice. 1972. Phytochrome: Chemical and physical properties and mechanism of action. Ann. Rev. Plant Physiol. 23:293-334.
- Rice, H. V., W. R. Briggs, and C. J. Jackson-White. 1973. Purification of oat and rye phytochrome. Plant Physiol. 51:917-926.
- Tobin, E. M. and W. R. Briggs. 1973. Studies on the protein conformation of phytochrome. Photochem. Photobiol. 18:487-495.
- Blatt, M. R., N. K. Wessells, and W. R. Briggs. 1980. Actin and cortical fiber reticulation in the siphonaceous alga Vaucheria sessilis. Planta 147:363-375.
- Mandoli, D. F. and W. R. Briggs. 1981. Phytochrome control of two low-irradiance responses in etiolated oat seedlings. Plant Physiol. 67: 733-739.
- Mandoli, D. F. and W. R. Briggs. 1982. Optical properties of etiolated plant tissues. Proc. Nat. Acad. Sci. U. S. A. 79:2902-2906.
- Iino, M. and W. R. Briggs. 1984. Growth distribution during first positive phototropic curvature of maize coleoptiles. Plant Cell Environ. 7:97-104.
- Kaufman, L. S., W. F. Thompson, and W. R. Briggs. 1984. Different red light requirements for phytochrome-induced accumulation of cab RNA and rbcS RNA. Science 226:1447-1449.
- Mösinger, E., A. Batschauer, K. Apel, E. Schäfer, and W. R. Briggs. 1988. Phytochrome regulation of greening in barley - effects on mRNA abundance and on transcriptional activity of isolated nuclei. Plant Physiol. 86:706-710.
- Gallagher, S., T. W. Short, L. H. Pratt, P. M. Ray, and W. R. Briggs. 1988. Light-induced changes in two proteins found associated with plasma membrane fractions from pea stem sections. Proc. Natl. Acad. Sci. U. S. A. 85:8003-8007.
- Short, T. W. and W. R. Briggs. 1990. Characterization of a rapid, blue light- mediated change in detectable phosphorylation of a plasma membrane protein from etiolated pea (Pisum sativum L.) seedlings. Plant Physiol. 92:179-185.
- Reymond, P., T. W. Short, W. R. Briggs, and K. L. Poff. 1992. Light-induced phosphorylation of a membrane protein plays an early role in signal transduction for phototropism in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U. S. A. 89: 4718-4721.
- Liscum, E. and W. R. Briggs. 1995. Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli. Plant Cell 7: 473-485.
- Huala, E., P. W. Oeller, E. Liscum, I.-S. Han, E. Larsen, and W. R. Briggs. 1997. Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain. Science 278: 2120-2123.
- Christie, J. M., P. Reymond, G. Powell, P. Bernasconi, A. A. Reibekas, E. Liscum, and W. R. Briggs. 1998. Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism. Science 282: 1698-1701.
- Briggs, W. R. and E. Huala. 1999. Blue-light photoreceptors in higher plants. Annu. Rev. Cell Dev. Biol. 15: 33-62.
- Salomon, M., J. M. Christie, E. Knieb, U. Lempert, and W. R. Briggs. 2000. Photochemical and mutational analysis of the FMN-binding domains of the plant blue light photoreceptor phototropin. Biochemistry 39: 9401-9410.
- Sakamoto, K. and W. R. Briggs. 2002. Cellular and subcellular localization of phototropin 1. Plant Cell 14: 1723-1735.
- Christie, J. M., T. E. Swartz, R. A. Bogomolni, and W. R. Briggs. 2002. Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J. 32: 205-219.
- Corchnoy, S. B., T. E. Swartz, J. W. Lewis, I. Szundi, W. R. Briggs, and R. A. Bogomolni. 2003. Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1. J. Biological Chemistry 278: 724-731.
- Briggs, W. R. 2006. Flavin-based photoreceptors in plants, in: Flavins Photochemistry and Photobiology, E. Silva, A. M. Edwards (eds.), Comprehensive Series in Photochemical and Photobiological Sciences, Donat-Peter Häder, Giulio Jori (Series eds.) RSC, Cambridge UK. Pp. 183-216.
- Swartz, T. E., T.-S. Tseng, M. A. Frederickson, G. Paris, D. J. Comerci, G. Rajeshekara, J.-G. Kim, M. B. Mudgett, G. Splitter, R. A. Ugalde, F. Goldbaum, W. R. Briggs, and R. A. Bogomolni. 2007. Blue light-activated histidine kinases: two-component sensors in bacteria. Science 317: 1090-1093.