Common amino acid sequence domains among the LEA proteins of higher plants

✍ Scribed by Leon Dure; Martha Crouch; John Harada; Tuan-Hua David Ho; John Mundy; Ralph Quatrano; Terry Thomas; Z. R. Sung

• Book ID: 104616897
• Publisher: Springer
• Year: 1989
• Tongue: English
• Weight: 660 KB
• Volume: 12
• Category: Article
• ISSN: 0167-4412
• DOI: 10.1007/bf00036962

✦ Synopsis

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 ct helix which may serve as the basis for higher order structure.