Structure and function of group 1 late embryogenesis abundant proteins

Transcription

1 Chinese Bulletin of Life Sciences Vol. 20, No. 3 Jun., (2008) (late embryogenesis abundant proteins LEA) LEA 6 1 LEA LEA1 20 LEA1 LEA1 LEA1 20 S565.1 Q946.1 A Structure and function of group 1 late embryogenesis abundant proteins ZOU Yong-dong, SHI Li-sha, LIU Guo-bao, HONG Rui-sha, ZHENG Yi-zhi* (College of Life Science, Shenzhen University, Shenzhen , China) Abstract: Late embryogenesis abundant proteins (LEA) accumulate to high concentrations in plant embryo during the later stage of seed development accompanied by dehydration. Based on the common amino acid sequence motif and the conserved structural features, LEA proteins are basically divided into six groups. Group 1 LEA proteins (LEA1) have an internal 20-residue amino acid motif and are largely unordered in solution, highly hydrophilic, heat-stable and associated with tolerance to water stress resulting from desiccation, cold shock and salt. Key words: LEA1 proteins; 20-residue amino acids motif; function; structure; promoter late embryogenesis abundant protein LEA 1981 Dure [1] Gosspypium hirsutum mrna Lea mrna LEA LEA [2-4] LEA [5-11] LEA 20 LEA [12-17] LEA [18-21] LEA LEA LEA 6 1 LEA (LEA1) [6,22-24] NCBI Genebank ( ) (ZJY03A18) (200621) * yzzheng@szu.edu.cn

2 Em Em LEA1 ( ) ( 1) LEA1 [25] 1 Genebank 20 Accession No. Length of Copy Name of polypeptide protein number Source in Genebank (aa) of motif AAC36329 late embryogenic abundant protein Vigna radiata AAB07225 Em 99 1 Vigna radiata AAB39473 Em Robinia pseudoacacia AAB39474 Em 99 1 Robinia pseudoacacia CAA33479 unnamed protein product 83 1 Raphanus sativus AAP97398 Em Quercus robur ABB13462 Em Medicago truncatula CAA kda Lea 92 1 Helianthus annuus S23527 embryonic abundant protein 92 1 Helianthus annuus AAB00728 water-stress protectant protein Gossypium hirsutum P09443 LEA D Gossypium hirsutum AAA92729 storage protein Gossypium hirsutum AAB71224 Em Glycine max AAB68027 D Glycine max BAD86646 Em-like protein Daucus carota BAD86647 EMB1 protein 92 1 Daucus carota CAA05711 Em 84 1 Brassica napus AAY54009 LEA protein 95 1 Arachis hypogaea AAZ20278 lea protein Arachis hypogaea NP_ ATEM Arabidopsis thaliana AAA62326 late embryogenic abundant protein Arabidopsis thaliana NP_ ATEM Arabidopsis thaliana AAA33458 LEA Zea mays CAA39063 embrygenic protein 91 1 Zea mays CAA65308 Em 93 1 Triticum aestivum CAB88091 Early-methionine-labelled polypeptide 90 1 Secale cereale CAB88093 Early-methionine-labelled polypeptide 93 1 Secale cereale AAV44066 LEA Oryza sativa CAA44624 LEA B Hordeum vulgare subsp. Vulgare CAA44623 LEA B Hordeum vulgare subsp. Vulgare CAA54402 gb19.1b 93 1 Hordeum vulgare subsp. vulgare CAA44622 LEA B Hordeum vulgare subsp. Vulgare BAD22769 embryonic abundant protein Bromus inermis BAD22768 embryonic abundant protein 94 1 Bromus inermis ABA54808 Em-like protein 91 1 Picea mariana AAB01568 Em-like protein 91 1 Picea glauca AAZ04476 group 1 LEA protein 88 1 Physcomitrella patens CAA40009 gsib Bacillus subtilis ZP_ hypothetical protein AvinDRAFT_ Azotobacter vinelandii AvOP EAL80001 Em-like protein GEA1 (EM1) 61 1 Anaeromyxobacter dehalogenans 2CP-C

3 LEA1 LEA1 LEA1 [26-30] LEA1 [31-32] 1.1 LEA1 Cheng [26] LEA1 PMA1959 (200 mm) ( ) LEA1 Em 1.5% NaCl [27] LEA1 ATEM6 [28] 1.2 LEA1 Swire-Clark Marcotte [29] LEA1 Em (1mol/L NaCl KCl) (1.5mol/L ) LEA1 Em (800mmol/LNaCl 700mmol/L KCl) 4 24h [30] LEA1 LEA1 LEA1 1.3 LEA1 Goyal [31] LEA1 Em (43 ) Gilles [32] LEA1 Em α 20 Em 20 [32] 20 Em 20 2 LEA1 LEA1 LEA1 McCubbin [33] LEA1 Em Em Eom [34] (H 1 -NMR) LEA1 EMB-1 Russouw [35] LEA1 p11 2% α- 80 Soulages [25] LEA1 (rgmd-19) Soulages [25] LEA1 rgmd % α β 8% 5% 50% 30%α- 1% 8% α % P (Poly-(lproline)-type) P P 14% 6% P Soulages LEA1P α- β- Gilles [32] LEA1 Em Soulages

4 492 Em ( 20 2 α- 7 1 α- 2 ) 20 Em Em LEA1 Em 60% 50% α- 26% 2mmol/L α- 28% 20 P ( ) LEA1 α- P 3 LEA1 LEA1 LEA1 LEA1 (molecular shield) (chaperones for water stress) [31] LEA1 P P C=O N-H P LEA1 [32] LEA1 α- LEA1 α- LEA1 [32] LEA1 P α- LEA1 LEA1 LEA1 LEA1 LEA1 4 LEA1 LEA1 Em TATA-box CAAT-box ABA 1 DRE1 2 ABRE 1 AG-motif 1 ELRE-motif 2 RY-repeat 1 TGTCACA- Motif Em [36] 5 LEA1 1 LEA1 20 Bacillus subtilis GsiB 4 20 [37] Azotobacter vinelandii AvOP AvinDRAFT_ LEA1 Wise [38] POPP(protein or oligonucleotide probability profile) LEA POPP ( ) LEA1 ( 2) LEA1 LEA1a LEA1b LEA 4(superfamily 4) 6 (superfamily 6) DNA [1] Dure L III, Greenway SC, Galau GA. Developmental bio-

5 POPP LEA1 [38] LEA LEA POPP 1a GGQTRRE 4 +E +G +EG +GE +GG H4 DNA QLGEEGY + K G +QE +RK +GGE DNA SQMGRK +KGG 1b 6 +E +G +DE +EG +ES RNA DNA - +GG +GQ +RE +RK (DNA) CLP ATP DNA +ARE +DES +REG + chemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and protein synthesis. Biochemistry, 1981, 20 (14): [2] Baker J, Steele C, Dure L III. Sequence and characterization of 6 Lea proteins and their genes from cotton. Plant Mol Biol, 1988, 11: [3] Dure L III, Crouch M, Harada J, et al. Common amino acid sequence domains among the LEA proteins of higher plants. Plant Mol Biol, 1989, 12: [4] Hughes DW, Galau GA. Temporally modular gene expression during cotyledon development. Genes Dev, 1989, 3: [5] Chandler PM, Robertson M. Gene expression regulated by abscisic acid and its relation to stress tolerance. Annu Rev Plant Physiol Plant Mol Biol, 1994, 45: [6] Ingram J, Bartels D. The molecular basis of dehydration tolerance in plants. Annu Rev Plant Physiol Plant Mol Biol, 1996, 47: [7] Bray EA. Plant responses to water deficit. Trends Plant Sci, 1997, 2: [8] Close TJ. Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant, 1996, 97: [9] Close TJ. Dehydrins: a commonalty in the response of plants to dehydration and low temperature. Physiol Plant, 1997, 100: [10] Thomashow MF. Role of cold-responsive genes in plant freezing tolerance. Plant Physiol, 1998, 118: 1-17 [11] Nylander M, Svensson J, Palva ET, et al. Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana. Plant Mol Biol, 2001, 45: [12] Reid JL, Walker-simmons MK. Group 3 late embryogenesis abundant proteins in desiccation-tolerant of wheat (Triticumaestivum L.). Plant Physiol, 1993, 102: [13] Colse TJ, Kortt AA, Chandler PM. A cdna-based comparison of dehydration-induced proteins (dehydrins) in barley and corn. Plant Mol Biol, 1989, 13: [14] Zegzouti H, Jones B, Marty C, et al. ER5, a tomato cdna encoding an ethylene-responsive LEA-like protein: Characterization and expression in response to drought, ABA and wounding. Plant Mol Biol, 1997, 35(6): [15] Hsing YC, Chen Z, Shih M, et al. Unusual sequence of group 3 LEA mrna inducible by maturation or drying in soybean seeds. Plant Mol Biol, 1995, 29: [16] Franz G, Hatzopoulos P, Jones TJ, et al. Molecular and genetic analysis of an embryonic gene, DC 8, from Daucus carota L. Mol Gen Genet, 1989, 218(1): [17] Roberts JK, DeSimone NA, Lingle WL, et al. Cellular concentrations and uniformity of cell-type accumulation of two lea proteins in cotton embryos. Plant Cell, 1993, 5: [18] Browne J, Tunnacliffe A, Burnell A. Anhydrobiosis: plant desiccation gene found in a nematode. Nature, 2002, 416: 38 [19] Browne JA, Dolan KM, Tyson T, et al. Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae. Eukaryot Cell, 2004, 3: [20] Tanaka S, Ikeda K, Miyasaka H. Isolation of a new member of group 3 late embryogenesis abundant protein from a halotolerant green alga by a functional expression screening with cyanobacterial cells. FEMS Microbiol Lett, 2004, 236: 41-5 [21] Makarova KS, Aravind L, Wolf YI, et al. Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics. Microbiol Mol Biol Rev, 2001, 65: [22] Dure L III. Structural motifs in Lea proteins[m]//. Close TJ, Bray EA, eds. Plant responses to cellular dehydration during environmental stress. Current topics in plant physiology, Vol 10. Rockville: American Society of Plant Physiologists, 1993: [23] Esperlund M, Saeboe-Larssen S, Hughes DW, et al. Late embryogenesis-abundant genes encoding proteins with different numbers of hydrophobic repeats are regulated differentially by abscisic acid and osmotic stress. Plant J, 1992, 2: [24] Burns W C, Maitra N, Cushman JC. Isolation and characterization of a cdna encoding a group 1 LEA protein(accession NO.U66317)from soybean1. Plant Physiol, 1997, 113:663 [25] Soulages JL, Kim K, Walters C, et al. Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. Plant Physiol, 2002, 128: [26] Cheng Z, Targolli J, Huang X, et al. Wheat LEA genes, PM80

6 494 and PMA1959, enhance dehydration tolerance of transgenic rice (Oryza sativa L.). Mol Breed, 2002, 10: [27]. LEA Em, 2006, 23(3): [28] Manfre AJ, Lanni LM, Marcotte WR Jr. The Arabidopsis group1 late embryogenesis abundant protein ATEM6 is required for normal seed development. Plant Physiol, 2005, 140: [29] Swire-Clark GA, Marcotte WR Jr. The wheat LEA protein Em functions as an osmoprotective molecule in Saccharomyces cerevisiae. Plant Mol Biol, 1999, 39: [30] Lan Y, Cai D, Zheng YZ. Expression of three different group soybean lea genes enhanced stress tolerance in Escherichia coli. J Integr Plant Biol, 2005, 42(5): [31] Goyal K, Walton LJ, Tunnacliffe A. LEA proteins prevent protein aggregation due to water stress. Biochem J, 2005, 388 (4): [32] Gilles GJ, Hines KM, Manfre AJ, et al. A predicted N- terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying. Plant Physiol Biochem, 2007, 45: [33] McCubbin WD, Kay CM, Lane BG. Hydrodynamic and optical properties of the wheat germ Em protein. Can J Biochem Cell Biol, 1985, 63: [34] Eom J, Baker WR, Kintanar A, et al. The embryo-specific EMB-1 protein of Daucus carota is flexible and unstructured in solution. Plant Sci, 1996, 115: [35] Russouw PS, Farrant J, Brandt W, et al. The most prevalent protein in a heat-treated extract of pea (Pisum sativum) embryos is an LEA group I protein; its conformation is not affected by exposure to high temperature. Seed Sci Res, 1997, 7: [36]. Em (LEA1)., 2007, 26(4): [37] Stacy RA, Aalen RB. Identification of sequence homology between the internal hydrophilic repeated motifs of Group 1 late-embryogenesis-abundant proteins in plants and hydrophilic repeats of the general stress protein GsiB of Bacillus subtilis. Planta, 1998, 206:476-8 [38] Wise MJ, Tunnacliffe A. POPP the question: what do LEA proteins do? Trends Plant Sci, 2004, 9(1): 13-7 Chinese Bulletin of Life Sciences Chinese Bulletin of Life Sciences (Bimonthly) ( )(1988 ) (Started in 1988) ( 120 ) Jun., 2008 Vol.20 No ( ) cbls@sibs.ac.cn ( ) ( 782 ) by Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences Edited by GUAN Xing-hua, YUE Dong-fang, YU Jian-rong Editorial Office of Chinese Bulletin of Life Sciences (319 Yueyang Road, Shanghai , China) Editor-in-Chief LIN Qi-shui Sponsored by Department of Life Sciences, National Natural Science Foundation of China; Bureau of Life Sciences and Biotechnology, Chinese Academy of Sciences; Division of Life Sciences and Medicine, Chinese Academy of Sciences; Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences Published by Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences Distributed by Shanghai Post Office Subscripted by Local Post Offices Overseas Distributed by China National Publishing Industry Trading Corporation (P.O.Box 782, Beijing, China) Cable: CNPITC ISSN CN /Q : : DK : 25.00