Search

Your search keyword '"Lai, Xuelei"' showing total 142 results
Start Over Author "Lai, Xuelei"
142 results on '"Lai, Xuelei"'

5. Flower Development in Arabidopsis

Author

Chahtane, Hicham, primary, Lai, Xuelei, additional, Tichtinsky, Gabrielle, additional, Rieu, Philippe, additional, Arnoux-Courseaux, Moïra, additional, Cancé, Coralie, additional, Marondedze, Claudius, additional, and Parcy, François, additional

Published
2023
Full Text
View/download PDF

8. SEPALLATA-driven MADS transcription factor tetramerization is required for inner whorl floral organ development

Author

Hugouvieux, Veronique, primary, Blanc-Mathieu, Romain, additional, Janeau, Aline, additional, Paul, Michel, additional, Lucas, Jeremy, additional, Xu, Xiaocai, additional, Ye, Hailong, additional, Lai, Xuelei, additional, LeHir, Sarah, additional, Guillotin, Audrey, additional, Galien, Antonin, additional, Yan, Wenhao, additional, Nanao, Max, additional, Kaufmann, Kerstin, additional, Parcy, François, additional, and Zubieta, Chloe, additional

Published
2024
Full Text
View/download PDF

9. Molecular mechanisms of Evening Complex activity in Arabidopsis

Author

Silva, Catarina S., Nayak, Aditya, Lai, Xuelei, Hutin, Stephanie, Hugouvieux, Véronique, Jung, Jae-Hoon, López-Vidriero, Irene, Franco-Zorrilla, Jose M., Panigrahi, Kishore C. S., Nanao, Max H., Wigge, Philip A., and Zubieta, Chloe

Published
2020

11. The OsSRO1c-OsDREB2B complex undergoes protein phase transition to enhance cold tolerance in rice.

Author

Hu, Dan, Yao, Yilong, Lv, Yan, You, Jun, Zhang, Yu, Lv, Qingya, Li, Jiawei, Hutin, Stephanie, Xiong, Haiyan, Zubieta, Chloe, Lai, Xuelei, and Xiong, Lizhong

Abstract

Cold stress is one of the major abiotic stress factors affecting rice growth and development, leading to significant yield loss in the context of global climate change. Exploring natural variants that confer cold resistance and the underlying molecular mechanism responsible for this is the major strategy to breed cold-tolerant rice varieties. Here, we show that natural variations of a SIMILAR to RCD ONE (SRO) gene, OsSRO1c , confer cold tolerance in rice at both seedling and booting stages. Our in vivo and in vitro experiments demonstrated that Os SRO1c possesses intrinsic liquid–liquid phase-separation ability and recruits Os DREB2B, an AP2/ERF transcription factor that functions as a positive regulator of cold stress, into its biomolecular condensates in the nucleus, resulting in elevated transcriptional activity of Os DREB2B. We found that the Os SRO1c- Os DREB2B complex directly responds to low temperature through dynamic phase transitions and regulates key cold-response genes, including COLD1. Furthermore, we showed that introgression of an elite haplotype of OsSRO1c into a cold-susceptible indica rice could significantly increase its cold resistance. Collectively, our work reveals a novel cold-tolerance regulatory module in rice and provides promising genetic targets for molecular breeding of cold-tolerant rice varieties. This study reveals that OsSRO1c possesses intrinsic liquid–liquid phase-separation properties and can enhance rice cold tolerance by interacting with the transcription factor OsDREB2B. The OsSRO1c-OsDREB2B complex undergoes cold-dependent phase transitions to upregulate the expression of key cold-response genes such as COLD1. Introducing an elite OsSRO1c haplotype into susceptible rice varieties significantly improves cold resistance, providing valuable targets for breeding cold-tolerant rice varieties. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

17. CircRNAs in Plants

Author

Lai, Xuelei, Bazin, Jérémie, Webb, Stuart, Crespi, Martin, Zubieta, Chloe, Conn, Simon J., COHEN, IRUN R., Series Editor, LAJTHA, ABEL, Series Editor, LAMBRIS, JOHN D., Series Editor, PAOLETTI, RODOLFO, Series Editor, Rezaei, Nima, Series Editor, and Xiao, Junjie, editor

Published
2018
Full Text
View/download PDF

19. SEPALLATA-driven MADS transcription factor tetramerization is required for inner whorl floral organ development

Author

Hugouvieux, Veronique Genevieve, primary, Blanc-Mathieu, Romain, additional, Paul, Michel, additional, Janeau, Aline, additional, Xu, Xiaocai, additional, Lucas, Jeremy, additional, Lai, Xuelei, additional, Galien, Antonin, additional, Yan, Wenhao, additional, Nanao, Max H, additional, Kaufmann, Kerstin, additional, Parcy, Francois, additional, and Zubieta, Chloë, additional

Published
2023
Full Text
View/download PDF

20. Source Data: A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis

Author

Jung, Jae-Hoon, Barbosa, Antonio, Hutin, Stephanie, Kumita, Janet, Gao, Mingjun, Derwort, Dorothee, Silva, Catarina, Lai, Xuelei, Pierre, Elodie, Geng, Feng, Kim, Sol-Bi, Baek, Sujeong, Zubieta, Chloe, Jaeger, Katja, and Wigge, Philip

Subjects
animal diseases, nervous system diseases
Abstract

Source data for "A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis"

Published
2022
Full Text
View/download PDF

21. Serine protease NAL1 exerts pleiotropic functions through degradation of TOPLESS-related corepressor in rice

Author

Li, Wenjing, primary, Yan, Junjie, additional, Zhang, Yu, additional, Zhang, Fei, additional, Guan, Zeyuan, additional, Yao, Yilong, additional, Chang, Yu, additional, Tu, Haifu, additional, Li, Xiaokai, additional, Wang, Huaijun, additional, Xiong, Haiyan, additional, Lai, Xuelei, additional, Yin, Ping, additional, and Xiong, Lizhong, additional

Published
2022
Full Text
View/download PDF

22. Distinct roles of MADS-box complexes in the control of the dormancy cycle in apple

Author

Falavigna, Vitor, Severing, Edouard, Lai, Xuelei, Hugouvieux, Véronique, Farrera, Isabelle, Garighan, Julio, Parcy, Francois, Zubieta, Chloe, Coupland, George, Costes, Evelyne, Andrés, Fernando, Amélioration génétique et adaptation des plantes méditerranéennes et tropicales (UMR AGAP), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Max Planck Institute for Plant Breeding Research (MPIPZ), Physiologie cellulaire et végétale (LPCV), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Grenoble Alpes (UGA)

Subjects
[SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BDD]Life Sciences [q-bio]/Development Biology
Abstract

International audience; Dormancy is an essential developmental program that allows tree adaptation to low temperatures by inducing a bud resting state until the end of the winter. After a prolonged cold period, buds reactivate growth in response to the warm temperatures of the spring. In many Rosaceae species, it is believed that a group of genes encoding MADS-box transcription factors controls dormancy cycle. These genes are similar to SHORT VEGETATIVE PHASE (SVP) from Arabidopsis thaliana and often referred as DORMANCY-ASSOCIATED MADS-BOX (DAM) genes. Although their potential role in tree phenology, the precise function and the mode of action of SVP-like genes during the dormancy cycle are still unknown. By making use of apple tree (Malus x domestica) as a model, we have investigated the function of rosaceous SVP-like genes. We found that most of them show patterns of expression that correlate with particular phases of the dormancy cycle. However, MdSVPa, a MADS-box gene that represses budbreak when it is overexpressed in apple, was ectopically expressed during the whole cycle. We also identified several potential complexes formed by apple MADS-box proteins and interestingly, only complexes containing MdSVPa were able to bind a DNA probe carrying two CArG boxes. In the light of these results, we hypothesized that MdSVPa is an essential component of the transcriptional complexes that regulate dormancy cycle. To unravel the roles of these complexes, we have made use of DNA Affinity Purification followed by massive parallel sequencing (DAP-seq). Our DAP-seq analyses showed that MdSVPa-containing complexes bind to gene targets involved in biological processes that could affect dormancy cycle, such as hormone signaling, cell wall and lignin modifications, sugar transport, cell cycle and flower development, among others. These results allow us to build a tentative model describing distinct roles of MADS-box complexes during the dormancy cycle in apple tree.

Published
2021

23. The Intervening Domain Is Required For DNA-binding and Functional Identity of Plant MADS Transcription Factors

Author

Lai, Xuelei, primary, Vega-Leon, Rosario, additional, Hugouvieux, Veronique, additional, Blanc-Mathieu, Romain, additional, Wal, Froukje van der, additional, Lucas, Jeremy, additional, Silva, Catarina, additional, Jourdain, Agnes, additional, Muino, Jose, additional, Nanao, Max, additional, Immink, Richard, additional, Kaufmann, Kerstin, additional, Parcy, Francois, additional, Smaczniak, Cezary, additional, and Zubieta, Chloe, additional

Published
2021
Full Text
View/download PDF

24. Unraveling the role of MADS transcription factor complexes in apple tree dormancy using sequential DAP-seq

Author

Falavigna, Vítor da Silveira, primary, Severing, Edouard, additional, Lai, Xuelei, additional, Estevan, Joan, additional, Farrera, Isabelle, additional, Hugouvieux, Véronique, additional, Revers, Luís Fernando, additional, Zubieta, Chloe, additional, Coupland, George, additional, Costes, Evelyne, additional, and Andrés, Fernando, additional

Published
2021
Full Text
View/download PDF

25. The LEAFY floral regulator displays pioneer transcription factor properties

Author

Lai, Xuelei, primary, Blanc-Mathieu, Romain, additional, GrandVuillemin, Loïc, additional, Huang, Ying, additional, Stigliani, Arnaud, additional, Lucas, Jérémy, additional, Thévenon, Emmanuel, additional, Loue-Manifel, Jeanne, additional, Daher, Hussein, additional, Brun-Hernandez, Eugenia, additional, Vachon, Gilles, additional, Latrasse, David, additional, Benhamed, Moussa, additional, Dumas, Renaud, additional, Zubieta, Chloe, additional, and Parcy, François, additional

Published
2021
Full Text
View/download PDF

27. Molecular mechanisms of Evening Complex activity in Arabidopsis

Author

Agence Nationale de la Recherche (France), European Molecular Biology Laboratory, European Commission, Université Grenoble Alpes, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Silva, Catarina S., Nayak, Aditya, Lai, Xuelei, Hutin, Stephanie, Hugouvieux, Véronique, Jung, Jae-Hoon, López-Vidriero, Irene, Franco-Zorrilla, José Manuel, Panigrahi, Kishore C. S., Nanao, Max H., Wigge, Philip A., Zubieta, Chloe, Agence Nationale de la Recherche (France), European Molecular Biology Laboratory, European Commission, Université Grenoble Alpes, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Silva, Catarina S., Nayak, Aditya, Lai, Xuelei, Hutin, Stephanie, Hugouvieux, Véronique, Jung, Jae-Hoon, López-Vidriero, Irene, Franco-Zorrilla, José Manuel, Panigrahi, Kishore C. S., Nanao, Max H., Wigge, Philip A., and Zubieta, Chloe

Abstract

The Evening Complex (EC), composed of the DNA binding protein LUX ARRHYTHMO (LUX) and two additional proteins EARLY FLOWERING 3 (ELF3) and ELF4, is a transcriptional repressor complex and a core component of the plant circadian clock. In addition to maintaining oscillations in clock gene expression, the EC also participates in temperature and light entrainment, acting as an important environmental sensor and conveying this information to growth and developmental pathways. However, the molecular basis for EC DNA binding specificity and temperature-dependent activity were not known. Here, we solved the structure of the DNA binding domain of LUX in complex with DNA. Residues critical for high-affinity binding and direct base readout were determined and tested via site-directed mutagenesis in vitro and in vivo. Using extensive in vitro DNA binding assays of LUX alone and in complex with ELF3 and ELF4, we demonstrate that, while LUX alone binds DNA with high affinity, the LUX–ELF3 complex is a relatively poor binder of DNA. ELF4 restores binding to the complex. In vitro, the full EC is able to act as a direct thermosensor, with stronger DNA binding at 4 °C and weaker binding at 27 °C. In addition, an excess of ELF4 is able to restore EC binding even at 27 °C. Taken together, these data suggest that ELF4 is a key modulator of thermosensitive EC activity.

Published
2020

28. Phenylthiourea binding to human tyrosinase-related protein 1

Author

Lai, Xuelei, Wichers, Harry J., Soler-Lopez, Montserrat, Dijkstra, Bauke W., Lai, Xuelei, Wichers, Harry J., Soler-Lopez, Montserrat, and Dijkstra, Bauke W.

Abstract

Tyrosinase-related protein 1 (TYRP1) is one of the three human melanogenic enzymes involved in the biosynthesis of melanin, a pigment responsible for the color of the skin, hair, and eyes. It shares high sequence identity with tyrosinase, but has two zinc ions in its active site rather than two copper ions as in tyrosinase. Typical tyrosinase inhibitors do not directly coordinate to the zinc ions of TYRP1. Here, we show, from an X-ray crystal structure determination, that phenylthiourea, a highly potent tyrosinase inhibitor, does neither coordinate the active site zinc ions, but binds differently from other structurally characterized TYRP1-inhibitor complexes. Its aromatic ring is directed outwards from the active site, apparently as a result from the absence of polar oxygen substituents that can take the position of water molecules bound in the active site. The compound binds via hydrophobic interactions, thereby blocking substrate access to the active site.

Published
2020

29. Molecular mechanisms of Evening Complex activity in Arabidopsis

Author

#NODATA#, 0000-0001-6769-7349, Silva, Catarina S., Nayak, Aditya, Lai, Xuelei, Hutin, Stephanie, Hugouvieux, Veronique, Jung, Jae-Hoon, Lopez-Vidriero, Irene, Franco-Zorrilla, José Manuel, Panigrahi, Kishore C. S., Nanao, Max H., Wigge, Philip A., Zubieta, Chloe, #NODATA#, 0000-0001-6769-7349, Silva, Catarina S., Nayak, Aditya, Lai, Xuelei, Hutin, Stephanie, Hugouvieux, Veronique, Jung, Jae-Hoon, Lopez-Vidriero, Irene, Franco-Zorrilla, José Manuel, Panigrahi, Kishore C. S., Nanao, Max H., Wigge, Philip A., and Zubieta, Chloe

Published
2020

30. Structure and activity studies of tyrosinases and related proteins

Author

Lai, Xuelei, Lai, Xuelei, Lai, Xuelei, and Lai, Xuelei

Abstract

The copper-containing enzyme tyrosinase catalyzes the conversion of tyrosine into DOPAquinone, which is the precursor of melanin in almost all organisms. In humans, melanin is an essential pigment that protects the skin and eyes against the UV radiation from the sun. Mutations in the genes of the melanin biosynthetic pathway cause oculocutaneous albinism, a group of autosomal recessive disorders characterized by reduced or absent production of melanin in the skin, hair and eyes. In this thesis, we investigated the structure and activity of tyrosinases and related proteins, including human tyrosinase (TYR), human tyrosinase related protein 1 (TYRP1), and mushroom tyrosinase-associated lectin-like protein (MtaL). TYR and TYRP1 are membrane-bound glycoproteins that occur in melanosomes. Using a baculovirus expression system in insect cells we succeeded in producing large amounts of the intramelanosomal domains of TYR and TYRP1, allowing their crystallization. Elucidation of the crystal structure of TYRP1 showed that TYRP1 contains zinc ions in its active site, in contrast to TYR which contains copper ions. This explains why TYRP1 does not have tyrosinase activity. The structure of TYRP1 is the first structure of a mammalian tyrosinase-like protein. Therefore, the TYRP1 structure makes it now possible to give detailed explanations of various albinism-causing mutations. In addition, the TYRP1 structure provides a solid base for the design of highly-desired compounds for pigmentation disorder treatments that reduce melanin production. Analysis of the MtaL structure suggests that the protein may have a carbohydrate-binding site allowing the protein to bind to a glycoreceptor.

Published
2017

33. Pioneer Factors in Animals and Plants—Colonizing Chromatin for Gene Regulation

Author

Lai, Xuelei, Verhage, Leonie, Hugouvieux, Veronique, Zubieta, Chloe, Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Action Thématique et Incitative sur Programme (ATIP)-Avenir, ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), ANR-16-CE92-0023,FLOPINET,Floral Pioneer Factors(2016), European Project: 609398, Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-10- LABX-49-01,Labex GRAL,Labex GRAL, and ANR-16-CE92-0023,FLOPINET,Floral Pioneer Factors

Subjects
Genome, pioneer activity, Transcription, Genetic, [SDV]Life Sciences [q-bio], education, Molecular Conformation, Gene Expression Regulation, Developmental, Cell Differentiation, Review, Plants, cell fate transition, Chromatin, humanities, Histones, lcsh:QD241-441, Eukaryotic Cells, lcsh:Organic chemistry, chromatin accessibility, Animals, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, health care economics and organizations, transcription factor, Transcription Factors
Abstract

International audience; Unlike most transcription factors (TF), pioneer TFs have a specialized role in binding closed regions of chromatin and initiating the subsequent opening of these regions. Thus, pioneer TFs are key factors in gene regulation with critical roles in developmental transitions, including organ biogenesis, tissue development, and cellular differentiation. These developmental events involve some major reprogramming of gene expression patterns, specifically the opening and closing of distinct chromatin regions. Here, we discuss how pioneer TFs are identified using biochemical and genome-wide techniques. What is known about pioneer TFs from animals and plants is reviewed, with a focus on the strategies used by pioneer factors in different organisms. Finally, the different molecular mechanisms pioneer factors used are discussed, highlighting the roles that tertiary and quaternary structures play in nucleosome-compatible DNA-binding.

Published
2018
Full Text
View/download PDF

34. Molecular mechanisms of Evening Complex activity in Arabidopsis

Author

Silva, Catarina S., primary, Nayak, Aditya, additional, Lai, Xuelei, additional, Hugouvieux, Veronique, additional, Jung, Jae-Hoon, additional, Jourdain, Agnès, additional, López-Vidriero, Irene, additional, Franco-Zorrilla, Jose Manuel, additional, Parcy, François, additional, Panigrahi, Kishore, additional, Wigge, Philip A., additional, Nanao, Max, additional, and Zubieta, Chloe, additional

Published
2019
Full Text
View/download PDF

39. The evening complex coordinates environmental and endogenous signals in Arabidopsis

Author

Ezer, Daphne, primary, Jung, Jae-Hoon, additional, Lan, Hui, additional, Biswas, Surojit, additional, Gregoire, Laura, additional, Box, Mathew S., additional, Charoensawan, Varodom, additional, Cortijo, Sandra, additional, Lai, Xuelei, additional, Stöckle, Dorothee, additional, Zubieta, Chloe, additional, Jaeger, Katja E., additional, and Wigge, Philip A., additional

Published
2017
Full Text
View/download PDF

40. Structure of Human Tyrosinase Related Protein 1 Reveals a Binuclear Zinc Active Site Important for Melanogenesis

Author

Lai, Xuelei, Wichers, Harry J., Soler-Lopez, Montserrat, Dijkstra, Bauke W., Lai, Xuelei, Wichers, Harry J., Soler-Lopez, Montserrat, and Dijkstra, Bauke W.

Abstract

Tyrosinase-related protein 1 (TYRP1) is one of three tyrosinase-like glycoenzymes in human melanocytes that are key to the production of melanin, the compound responsible for the pigmentation of skin, eye, and hair. Difficulties with producing these enzymes in pure form have hampered the understanding of their activity and the effect of mutations that cause albinism and pigmentation disorders. Herein we show that the typical tyrosinase-like subdomain of TYRP1 contains two zinc ions in the active site instead of copper ions as found in tyrosinases, which explains why TYRP1 does not exhibit tyrosinase redox activity. In addition, the structures reveal for the first time that the Cys-rich subdomain, which is unique to vertebrate melanogenic proteins, has an epidermal growth factor-like fold and is tightly associated with the tyrosinase subdomain. Our structures suggest that most albinism-related mutations of TYRP1 affect its stability or activity.

Published
2017

47. Structure and Function of Human Tyrosinase and Tyrosinase-Related Proteins.

Author

Lai, Xuelei, Wichers, Harry J., Soler‐Lopez, Montserrat, and Dijkstra, Bauke W.

Subjects
*MELANINS, *PHENOL oxidase, *TYRP1 gene, *METALLOENZYMES, *CRYSTAL structure
Abstract

Melanin is the main pigment responsible for the color of human skin, hair and eye. Its biosynthesis requires three melanogenic enzymes, tyrosinase (TYR), and the tyrosinase-related proteins TYRP1 and TYRP2. The difficulty of isolating pure and homogeneous proteins from endogenous sources has hampered their study, and resulted in many contradictory findings regarding their physiological functions. In this review, we summarize recent advances on the structure and function of TYR and TYRPs by virtue of the crystal structure of human TYRP1, which is the first available structure of a mammalian melanogenic enzyme. This structure, combined with tyrosinase structures from other lower eukaryotes and mutagenesis studies of key active site residues, sheds light on the mechanism of TYR and TYRPs. Furthermore, a TYRP1-based homology model of TYR provides a high-quality platform to map and analyze albinism-related mutations, as well as the design of specific antimelanogenic compounds. Finally, we provide perspectives for future structure/function studies of TYR and TYRPs. [ABSTRACT FROM AUTHOR]

Published
2018
Full Text
View/download PDF

48. Crystal structure of recombinant tyrosinase-binding protein MtaL at 1.35 Å resolution.

Author

Dijkstra, Bauke W., Lai, Xuelei, Soler-Lopez, Montserrat, Ismaya, Wangsa T., and Wichers, Harry J.

Subjects
*PHENOL oxidase, *LECTINS, *PROTEIN crystallography
Abstract

Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is unknown. In this study, the crystal structure of recombinant MtaL is reported at 1.35 Å resolution. Comparison of its structure with that of the truncated and cleaved MtaL present in the complex with tyrosinase directly isolated from mushroom shows that the general β-trefoil fold is conserved. However, differences are detected in the loop regions, particularly in the β2-β3 loop, which is intact and not cleaved in the recombinant MtaL. Furthermore, the N-terminal tail is rotated inwards, covering the tyrosinase-binding interface. Thus, MtaL must undergo conformational changes in order to bind mature mushroom tyrosinase. Very interestingly, the β-trefoil fold has been identified to be essential for carbohydrate interaction in other lectin-like proteins. Comparison of the structures of MtaL and a ricin-B-like lectin with a bound disaccharide shows that MtaL may have a similar carbohydrate-binding site that might be involved in glycoreceptor activity. [ABSTRACT FROM AUTHOR]

Published
2016
Full Text
View/download PDF

50. A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis

Author

Jung, Jae-Hoon, Barbosa, Antonio D, Hutin, Stephanie, Kumita, Janet R, Gao, Mingjun, Derwort, Dorothee, Silva, Catarina S, Lai, Xuelei, Pierre, Elodie, Geng, Feng, Kim, Sol-Bi, Baek, Sujeong, Zubieta, Chloe, Jaeger, Katja E, and Wigge, Philip A

Subjects
Models, Molecular, Repressor Proteins, Hot Temperature, Protein Domains, 13. Climate action, Arabidopsis Proteins, Acclimatization, Arabidopsis, Temperature, Peptides, Phase Transition, Prion Proteins, Transcription Factors
Abstract

Temperature controls plant growth and development, and climate change has already altered the phenology of wild plants and crops1. However, the mechanisms by which plants sense temperature are not well understood. The evening complex is a major signalling hub and a core component of the plant circadian clock2,3. The evening complex acts as a temperature-responsive transcriptional repressor, providing rhythmicity and temperature responsiveness to growth through unknown mechanisms2,4-6. The evening complex consists of EARLY FLOWERING 3 (ELF3)4,7, a large scaffold protein and key component of temperature sensing; ELF4, a small α-helical protein; and LUX ARRYTHMO (LUX), a DNA-binding protein required to recruit the evening complex to transcriptional targets. ELF3 contains a polyglutamine (polyQ) repeat8-10, embedded within a predicted prion domain (PrD). Here we find that the length of the polyQ repeat correlates with thermal responsiveness. We show that ELF3 proteins in plants from hotter climates, with no detectable PrD, are active at high temperatures, and lack thermal responsiveness. The temperature sensitivity of ELF3 is also modulated by the levels of ELF4, indicating that ELF4 can stabilize the function of ELF3. In both Arabidopsis and a heterologous system, ELF3 fused with green fluorescent protein forms speckles within minutes in response to higher temperatures, in a PrD-dependent manner. A purified fragment encompassing the ELF3 PrD reversibly forms liquid droplets in response to increasing temperatures in vitro, indicating that these properties reflect a direct biophysical response conferred by the PrD. The ability of temperature to rapidly shift ELF3 between active and inactive states via phase transition represents a previously unknown thermosensory mechanism.

Catalog

Books, media, physical & digital resources
See catalog results