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Common amino acid sequence domains among the LEA proteins of higher plants |
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| Authors: | Leon Dure III Martha Crouch John Harada Tuan-Hua David Ho John Mundy Ralph Quatrano Terry Thomas Z. R. Sung |
| Affiliation: | (1) Department of Biochemistry, University of Georgia, 30602 Athens, GA, USA;(2) Department of Biology, Indiana University, 47405 Bloomington, IN, USA;(3) Department of Botany, University of California, 95616 Davis, CA, USA;(4) Biology Department, Washington University, 63130 St. Louis, MO, USA;(5) Laboratory of Plant Molecular Biology, The Rockefeller University, 1230 York Avenue, 10021 New York, NY, USA;(6) Department of Biology, University of North Carolina, 27549 Chapel Nill, NC, USA;(7) Department of Biology, Texas A & M University, 77843 College Station, TX, USA;(8) Department of Genetics, University of California, 94720 Berkeley, CA, USA;(9) Department of Plant Pathology, University of California, 94720 Berkeley, CA, USA |
| Abstract: | LEA proteins are late embryogenesis abundant in the seeds of many higher plants and are probably universal in occurrence in plant seeds. LEA mRNAs and proteins can be induced to appear at other stages in the plant's life by desiccation stress and/or treatment with the plant hormone abscisic acid (ABA). A role in protecting plant structures during water loss is likely for these proteins, with ABA functioning in the stress transduction process. Presented here are conserved tracts of amino acid sequence among LEA proteins from several species that may represent domains functionally important in desiccation protection. Curiously, an 11 amino acid sequence motif is found tandemly repeated in a group of LEA proteins of vastly different sizes. Analysis of this motif suggests that it exists as an amphiphilic  helix which may serve as the basis for higher order structure. |
| Keywords: | LEA protein sequence plant desiccation abscisic acid |
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