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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 407487
Title OsLEA1a, a New Em-Like Protein of Cereal Plants
Author(s) Shih, M.D.; Huang, L.T.; Wei, F.J.; Wu, M.T.; Hoekstra, F.A.; Hsing, Y.I.C.
Source Plant and Cell Physiology 51 (2010)12. - ISSN 0032-0781 - p. 2132 - 2144.
DOI http://dx.doi.org/10.1093/pcp/pcq172
Department(s) Laboratory of Plant Physiology
EPS
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) embryogenesis-abundant protein - shrimp artemia-franciscana - abscisic-acid-response - lea messenger-rnas - gene-expression - seed maturation - desiccation tolerance - arabidopsis-thaliana - secondary structure - circular-dichroism
Abstract Proteins abundant in seeds during the late stages of development, late embryogenesis abundant (LEA) proteins, are associated with desiccation tolerance. More than 100 of the group I LEA genes, also termed Em genes, have been identified from plants, bacteria and animals. The wide distribution indicates the functional importance of these genes. In the present study, we characterized a novel Em-like gene, OsLEA1a of rice (Oryza sativa). 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 location of the sole intron indicates that the second exon of OsLEA1a is the mutated product of a typical Em gene. Transcriptome analysis revealed OsLEA1a mainly expressed in embryos, with no or only a few transcripts in osmotic stress-treated vegetative tissues. Structural analysis revealed that the OsLEA1a protein adopts high amounts of disordered conformations in solution and undergoes desiccation-induced conformational changes. Macromolecular interaction studies revealed that OsLEA1a 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. However, the protein does not function as a chaperone as do other groups of hydrophilic LEA proteins. 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.
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