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

• Published in: Planta Vol. 206; no. 3; pp. 476 - 478
• Main Authors: Stacy, R.A.P, Aalen, R.B
• Format: Journal Article
• Language: English
• Published: Berlin Springer-Verlag 01.10.1998; Springer
• Subjects: Agronomy. Soil science and plant productions; Amino Acid Sequence; amino acid sequences; Amino acids; Bacillus; Bacillus subtilis; Bacillus subtilis - chemistry; bacterial proteins; Bacterial Proteins - chemistry; Barley; Biological and medical sciences; chemical structure; Classical and quantitative genetics. Population genetics. Molecular genetics; Complementary DNA; desiccation; Embryogenesis; Fundamental and applied biological sciences. Psychology; Generalities. Genetics. Plant material; Genes; Genes. Genome; Genetics and breeding of economic plants; Heat shock proteins; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Open reading frames; plant proteins; Plant Proteins - chemistry; plants; Rapid Communication; Sequence Homology, Amino Acid; species differences; water stress; Repetitive DNA; Embryonic development; Monocotyledones; Hordeum vulgare; Bacillus subtilis; Homology; Identification; Bacillaceae; Water stress; Cereal crop; Hydrophily; Bacillales; Gramineae; Angiospermae; Heat shock protein; Bacteria; Spermatophyta; Protection; Comparative study; Aminoacid sequence
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/s004250050424

Late embryogenesis abundant (LEA) proteins are speculated to protect against water stress in plants. Group 1 LEA proteins are hydrophilic and vary mainly in the numbers of an extremely hydrophilic internal 20-amino-acid motif. This motif is present up to four times in Arabidopsis thaliana and Hordeum vulgare thaliana and Hordeum vulgare Group 1 proteins and has been described in numerous plant species. However, no similarity has yet been described between Group 1 genes or gene products and those from non-plant species. We report here the striking similarity between the repeated internal motif of Group 1 LEA proteins and a repeated hydrophilic motif present in a stress-related protein (GsiB) from Bacillus subtilis.