Late Embryogenesis Abundant (LEA) proteins, a group of hydrophilic proteins, have been linked to survival in plants and animals in periods of stress, putatively through safeguarding enzymatic function and prevention o...Late Embryogenesis Abundant (LEA) proteins, a group of hydrophilic proteins, have been linked to survival in plants and animals in periods of stress, putatively through safeguarding enzymatic function and prevention of aggregation in times of dehydration/heat. Yet despite decades of effort, the molecular-level mechanisms defining this protective function remain unknown. In this paper, we summarize and review research discoveries of the classification of the LEA protein groups based on their amino acid sequence similarity and on the presence of distinctive conserved motifs. Moreover, we focus on high correlation between their accumulation and water deficit, reinforcing their functional relevance under abiotic stresses. We also discuss the biochemical properties of LEA proteins arising from their hydrophilic nature and by amino acid composition. Although significant similarities have not been found between the members of the different groups, a unifying and outstanding feature of most of them is their high hydrophilicity and high content of glycine. Therefore, we have highlighted the biotechnological applications of LEA genes, and the effects of over-expressing LEA genes from all LEA groups from different species of origin into different plant hosts. Apart from agronomical purposes, LEA proteins could be useful for other biotechnological applications in relation to their capacity to prevent aggregation of proteins.展开更多
We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukar...We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukaryotic ceils showed a slower migration rate on SDS-PAGE gel. In addition, Rwddl was more sensitive to proteinase proteolysis. Furthermore, being a highly acidic protein which contains an RWD domain, Rwddl shared a high level of sequence similarity with Gir2, a member of the intrinsically unstructured protein （IUP）. These findings suggest that Rwddl is a novel member of the IUP family.展开更多
A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- ter...A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- terminal parts with each containing 30 amino acid （AA） residues and the middle region containing the remaining AA residues. The results show that in terminal parts, the percentage of disor- dered AA residues is higher than that of all AA residues （17% of disordered AA residues and 11% of all）. We analyzed the percentage of disorder for each of 20 AA residues in the three parts of proteins with respect to their hydropathy and molecular weight. For each AA, the percentage of disorder in the middle part is lower than that in terminal parts which is comparable at the two termini. A new scale of AAs has been introduced according to their disorder content in the middle part of proteins： CIFWMLYHRNVTAGQDSKEP. All big hydrophobic AAs are less frequently disordered, while almost all small hydrophilic AAs are more frequently disordered. The results obtained may be useful for construction and improving predictors for protein disorder.展开更多
基金supported jointly by grants from the Ministry of Higher Education and Scientific Research,Tunisia and the Agence Espagnole de cooperation Internationale(AECI)Officina Tecnica de Cooperacion,Spain
文摘Late Embryogenesis Abundant (LEA) proteins, a group of hydrophilic proteins, have been linked to survival in plants and animals in periods of stress, putatively through safeguarding enzymatic function and prevention of aggregation in times of dehydration/heat. Yet despite decades of effort, the molecular-level mechanisms defining this protective function remain unknown. In this paper, we summarize and review research discoveries of the classification of the LEA protein groups based on their amino acid sequence similarity and on the presence of distinctive conserved motifs. Moreover, we focus on high correlation between their accumulation and water deficit, reinforcing their functional relevance under abiotic stresses. We also discuss the biochemical properties of LEA proteins arising from their hydrophilic nature and by amino acid composition. Although significant similarities have not been found between the members of the different groups, a unifying and outstanding feature of most of them is their high hydrophilicity and high content of glycine. Therefore, we have highlighted the biotechnological applications of LEA genes, and the effects of over-expressing LEA genes from all LEA groups from different species of origin into different plant hosts. Apart from agronomical purposes, LEA proteins could be useful for other biotechnological applications in relation to their capacity to prevent aggregation of proteins.
基金a grant from theJapan Institute for the Control of Aging (JaICA 2000-2003)a fund from the National Natural Science Foundation of China (No. 30471589) to Dr. Wei He.
文摘We had previously identified a novel protein termed Rwddl whose expression in thymus is decreased in aged or oxidatively stressed mice. In the present study, we found that Rwddl expressed in both prokaryotic and eukaryotic ceils showed a slower migration rate on SDS-PAGE gel. In addition, Rwddl was more sensitive to proteinase proteolysis. Furthermore, being a highly acidic protein which contains an RWD domain, Rwddl shared a high level of sequence similarity with Gir2, a member of the intrinsically unstructured protein （IUP）. These findings suggest that Rwddl is a novel member of the IUP family.
基金supported by the Ministry of Education and Science,Republic of Serbia(Project No. 174021)
文摘A bioinformatics analysis of disorder content of proteins from the DisProt database has been performed with respect to position of dis- ordered residues. Each protein chain was divided into three parts： N- and C- terminal parts with each containing 30 amino acid （AA） residues and the middle region containing the remaining AA residues. The results show that in terminal parts, the percentage of disor- dered AA residues is higher than that of all AA residues （17% of disordered AA residues and 11% of all）. We analyzed the percentage of disorder for each of 20 AA residues in the three parts of proteins with respect to their hydropathy and molecular weight. For each AA, the percentage of disorder in the middle part is lower than that in terminal parts which is comparable at the two termini. A new scale of AAs has been introduced according to their disorder content in the middle part of proteins： CIFWMLYHRNVTAGQDSKEP. All big hydrophobic AAs are less frequently disordered, while almost all small hydrophilic AAs are more frequently disordered. The results obtained may be useful for construction and improving predictors for protein disorder.
