Difference between revisions of "Os01g0159600"
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Please input one-sentence summary here. | Please input one-sentence summary here. | ||
| − | + | Proteins abundant in seeds during the late stages of development, late embryogenesis abundant (LEA) proteins, are associated with desiccation tolerance. | |
==Annotated Information== | ==Annotated Information== | ||
===Function=== | ===Function=== | ||
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| + | 1.Several functional studies showed that the accumulation of LEA proteins might improve plant survival during osmotic stress. | ||
| + | 2.the accumulation of LEA proteins is tightly associated with the accumulation of non-reducing sugars, such as sucrose and raffi nose. | ||
| + | 3.LEA proteins were involved in the formation of glasses, the relationship between LEA proteins and non-reducing sugars is important in desiccation tolerance. | ||
===Expression=== | ===Expression=== | ||
Please input expression information here. | Please input expression information here. | ||
| + | The encoded OsLEA1a protein has an N-terminal sequence similar to that of other plant Em proteins but lacks a 20-mer motif that is the most significant feature of typical Em proteins. The similarity in the N-terminus between Em-like and typical Em proteins can be 60–80 %, depending on the species. The location of the sole intron indicates that the second exon of OsLEA1a is the mutated product of a typical Emgene. Transcriptome analysis revealed OsLEA1amainly expressed in embryos, with no or only a few transcripts in osmotic stress-treated vegetative tissues. the OsLEA1a protein adopts high amounts of disordered conformations in solution and undergoes desiccation-induced conformational changes. And the protein interacts with non-reducing sugars and phospholipids but not poly- L-lysine, Thus, although the OsLEA1a protein lost its 20-mer motif, it is still involved in the formation of bioglasses with non-reducing sugars or plasma membrane. | ||
===Evolution=== | ===Evolution=== | ||
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Please input evolution information here. | Please input evolution information here. | ||
| − | + | The orthologs of the OsLEA1a gene had been indentified from various grasses but not in dicot plants. Genetic analysis indicated that rice OsLEA1a locates at a 193 kb segment in chromosome 1 and is conserved in several published cereal genomes. Thus, the ancestor of Em-like genes might have evolved after the divergence of monocot plants. | |
You can also add sub-section(s) at will. | You can also add sub-section(s) at will. | ||
==Labs working on this gene== | ==Labs working on this gene== | ||
Please input related labs here. | Please input related labs here. | ||
| − | + | 1.Institute of Plant and Microbial Biology, Academia Sinica, Taipei, 11529, Taiwan, ROC. | |
| + | 2.Laboratory of Plant Physiology, Wageningen University, Wageningen, PO Box 658, NL-6700 AR, The Netherlands. | ||
==References== | ==References== | ||
Please input cited references here. | Please input cited references here. | ||
Ming-Der Shih; Lin-Tzu Huang; Fu-Jin Wei; Ming-Tsung Wu; Folkert A. Hoekstra; Yue-Ie C. Hsing (2010). OsLEA1a, a new Em-like protein of cereal plants. Plant and Cell Physiology, 51(12): 2132-2144. | Ming-Der Shih; Lin-Tzu Huang; Fu-Jin Wei; Ming-Tsung Wu; Folkert A. Hoekstra; Yue-Ie C. Hsing (2010). OsLEA1a, a new Em-like protein of cereal plants. Plant and Cell Physiology, 51(12): 2132-2144. | ||
==Structured Information== | ==Structured Information== | ||
| − | + | [[Category:Genes]][[Category:Oryza Sativa Japonica Group]][[Category:Japonica Chromosome 1]] | |
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Latest revision as of 04:33, 14 May 2015
Please input one-sentence summary here. Proteins abundant in seeds during the late stages of development, late embryogenesis abundant (LEA) proteins, are associated with desiccation tolerance.
Contents
Annotated Information
Function
1.Several functional studies showed that the accumulation of LEA proteins might improve plant survival during osmotic stress. 2.the accumulation of LEA proteins is tightly associated with the accumulation of non-reducing sugars, such as sucrose and raffi nose. 3.LEA proteins were involved in the formation of glasses, the relationship between LEA proteins and non-reducing sugars is important in desiccation tolerance.
Expression
Please input expression information here.
The encoded OsLEA1a protein has an N-terminal sequence similar to that of other plant Em proteins but lacks a 20-mer motif that is the most significant feature of typical Em proteins. The similarity in the N-terminus between Em-like and typical Em proteins can be 60–80 %, depending on the species. The location of the sole intron indicates that the second exon of OsLEA1a is the mutated product of a typical Emgene. Transcriptome analysis revealed OsLEA1amainly expressed in embryos, with no or only a few transcripts in osmotic stress-treated vegetative tissues. the OsLEA1a protein adopts high amounts of disordered conformations in solution and undergoes desiccation-induced conformational changes. And the protein interacts with non-reducing sugars and phospholipids but not poly- L-lysine, Thus, although the OsLEA1a protein lost its 20-mer motif, it is still involved in the formation of bioglasses with non-reducing sugars or plasma membrane.
Evolution
Please input evolution information here. The orthologs of the OsLEA1a gene had been indentified from various grasses but not in dicot plants. Genetic analysis indicated that rice OsLEA1a locates at a 193 kb segment in chromosome 1 and is conserved in several published cereal genomes. Thus, the ancestor of Em-like genes might have evolved after the divergence of monocot plants. You can also add sub-section(s) at will.
Labs working on this gene
Please input related labs here. 1.Institute of Plant and Microbial Biology, Academia Sinica, Taipei, 11529, Taiwan, ROC. 2.Laboratory of Plant Physiology, Wageningen University, Wageningen, PO Box 658, NL-6700 AR, The Netherlands.
References
Please input cited references here. Ming-Der Shih; Lin-Tzu Huang; Fu-Jin Wei; Ming-Tsung Wu; Folkert A. Hoekstra; Yue-Ie C. Hsing (2010). OsLEA1a, a new Em-like protein of cereal plants. Plant and Cell Physiology, 51(12): 2132-2144.
