Untitled

Hsing, Yue‐Ie C.; Tsou, Chen‐Lu; Hsu, Tze-Fu; Chen, Zuey-ying; Hsieh, Kim-leong; Hsieh, Jen-Wei; Chow, Teh-Yuan

doi:10.1023/a:1006079926339

Cited by 30 publications

(14 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast to most seed maturation proteins, protein PM36 contains a TENA_THI-4 conservative domain. It was predicted that PM36, similarly to seed maturation protein PM4, acted as a storage form of biotin to support seedling growth during germination (Hsing et al, 1998). In the present study, PM36 was up-regulated by salt in N2899.…”

Section: Differentially Expressed Proteinssupporting

confidence: 51%

See 1 more Smart Citation

Proteomic analysis of seed germination under salt stress in soybeans

Fan

Zheng

et al. 2011

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

Soybean (Glycine max (L.) Merrill) is a salt-sensitive crop, and its production is severely affected by saline soils. Therefore, the response of soybean seeds to salt stress during germination was investigated at both physiological and proteomic levels. The salt-tolerant cultivar Lee68 and salt-sensitive cultivar N2899 were exposed to 100 mmol/L NaCl until radicle protrusion from the seed coat. In both cultivars, the final germination percentage was not affected by salt, but the mean germination times of Lee68 and N2899 were delayed by 0.3 and 1.0 d, respectively, compared with controls. In response to salt stress, the abscisic acid content increased, and gibberellic acid (GA 1+3 ) and isopentenyladenosine decreased. Indole-3-acetic acid increased in Lee68, but remained unchanged in N2899. The proteins extracted from germinated seeds were separated using two-dimensional gel electrophoresis (2-DE), followed by Coomassie brilliant blue G-250 staining. About 350 protein spots from 2-DE gels of pH range 3 to 10 and 650 spots from gels of pH range 4 to 7 were reproducibly resolved, of which 18 protein spots showed changes in abundance as a result of salt stress in both cultivars. After matrix-assisted laser desorption ionization-time of flight-mass spectroscopy (MALDI-TOF-MS) analysis of the differentially expressed proteins, the peptide mass fingerprint was searched against the soybean UniGene database and nine proteins were successfully identified. Ferritin and 20S proteasome subunit β-6 were up-regulated in both cultivars. Glyceraldehyde 3-phosphate dehydrogenase, glutathione S-transferase (GST) 9, GST 10, and seed maturation protein PM36 were down-regulated in Lee68 by salt, but still remained at a certain level. However, these proteins were present in lower levels in control N2899 and were up-regulated under salt stress. The results indicate that these proteins might have important roles in defense mechanisms against salt stress during soybean seed germination.

show abstract

Section: Differentially Expressed Proteinssupporting

confidence: 51%

“…Spot 15 was identified as seed maturation protein PM36. It is synthesized at late embryogenesis and is degraded rapidly at the early stage of seed germination (Blackman et al, 1991;Hsing et al, 1998). In contrast to most seed maturation proteins, protein PM36 contains a TENA_THI-4 conservative domain.…”

Section: Differentially Expressed Proteinsmentioning

confidence: 99%

Proteomic analysis of seed germination under salt stress in soybeans

Fan

Zheng

et al. 2011

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

show abstract

“…An additional 13% correspond to putative uncharacterized proteins. Late embryogenesis proteins and maturation proteins represent 7% of the proteins, including Q39871_SOYBN (0.34% TSP), P93165_SOYBN Em protein (0.2% TSP) and Q9LLQ6_SOYBN seed maturation protein (0.13% TSP) [36,37]. These results are in agreement with those of other studies [15,17,20,32].…”

Section: Resultssupporting

confidence: 91%

NanoUPLC-MSE proteomic data assessment of soybean seeds using the Uniprot database

Murad

Rech

2012

BMC Biotechnol

View full text Add to dashboard Cite

BackgroundRecombinant DNA technology has been extensively employed to generate a variety of products from genetically modified organisms (GMOs) over the last decade, and the development of technologies capable of analyzing these products is crucial to understanding gene expression patterns. Liquid chromatography coupled with mass spectrometry is a powerful tool for analyzing protein contents and possible expression modifications in GMOs. Specifically, the NanoUPLC-MSE technique provides rapid protein analyses of complex mixtures with supported steps for high sample throughput, identification and quantization using low sample quantities with outstanding repeatability. Here, we present an assessment of the peptide and protein identification and quantification of soybean seed EMBRAPA BR16 cultivar contents using NanoUPLC-MSE and provide a comparison to the theoretical tryptic digestion of soybean sequences from Uniprot database.ResultsThe NanoUPLC-MSE peptide analysis resulted in 3,400 identified peptides, 58% of which were identified to have no miscleavages. The experiment revealed that 13% of the peptides underwent in-source fragmentation, and 82% of the peptides were identified with a mass measurement accuracy of less than 5 ppm. More than 75% of the identified proteins have at least 10 matched peptides, 88% of the identified proteins have greater than 30% of coverage, and 87% of the identified proteins occur in all four replicates. 78% of the identified proteins correspond to all glycinin and beta-conglycinin chains.The theoretical Uniprot peptide database has 723,749 entries, and 548,336 peptides have molecular weights of greater than 500 Da. Seed proteins represent 0.86% of the protein database entries. At the peptide level, trypsin-digested seed proteins represent only 0.3% of the theoretical Uniprot peptide database. A total of 22% of all database peptides have a pI value of less than 5, and 25% of them have a pI value between 5 and 8. Based on the detection range of typical NanoUPLC-MSE experiments, i.e., 500 to 5000 Da, 64 proteins will not be identified.ConclusionsNanoUPLC-MSE experiments provide good protein coverage within a peptide error of 5 ppm and a wide MW detection range from 500 to 5000 Da. A second digestion enzyme should be used depending on the tissue or proteins to be analyzed. In the case of seed tissue, trypsin protein digestion results offer good databank coverage. The Uniprot database has many duplicate entries that may result in false protein homolog associations when using NanoUPLC-MSE analysis. The proteomic profile of the EMBRAPA BR-16 seed lacks certain described proteins relative to the profiles of transgenic soybeans reported in other works.

show abstract

“…More importantly, it has been demonstrated that their expression may be significantly induced under abiotic stress conditions, such as cold, heat, and drought 15,24,25 . It has been proposed that LEA proteins may be involved in various important functions against abiotic stresses, including the stabilization of membrane structures 2,26,27 , the scavenging free radicals 28,29 , and the sequestering ions 29,30 or biotin 31 etc. At the cellular level, a subcellular location analysis revealed that LEA proteins are mainly located in the nucleus and the cytoplasm 32 .…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification and expression analyses of the LEA protein gene family in tea plant reveal their involvement in seed development and abiotic stress responses

Jin

Cao

Wang

et al. 2019

Sci Rep

View full text Add to dashboard Cite

Late embryogenesis abundant (LEA) proteins are widely known to be present in higher plants and are believed to play important functional roles in embryonic development and abiotic stress responses. However, there is a current lack of systematic analyses on the LEA protein gene family in tea plant. In this study, a total of 48 LEA genes were identified using Hidden Markov Model profiles in C. sinensis, and were classified into seven distinct groups based on their conserved domains and phylogenetic relationships. Genes in the CsLEA_2 group were found to be the most abundant. Gene expression analyses revealed that all the identified CsLEA genes were expressed in at least one tissue, and most had higher expression levels in the root or seed relative to other tested tissues. Nearly all the CsLEA genes were found to be involved in seed development, and thirty-nine might play an important role in tea seed maturation concurrent with dehydration. However, only sixteen CsLEA genes were involved in seed desiccation, and furthermore, most were suppressed. Additionally, forty-six CsLEA genes could be induced by at least one of the tested stress treatments, and they were especially sensitive to high temperature stress. Furthermore, it was found that eleven CsLEA genes were involved in tea plant in response to all tested abiotic stresses. Overall, this study provides new insights into the formation of CsLEA gene family members and improves our understanding on the potential roles of these genes in normal development processes and abiotic stress responses in tea plant, particularly during seed development and desiccation. These results are beneficial for future functional studies of CsLEA genes that will help preserve the recalcitrant tea seeds for a long time and genetically improve tea plant.

show abstract

Untitled

Cited by 30 publications

References 26 publications

Proteomic analysis of seed germination under salt stress in soybeans

Proteomic analysis of seed germination under salt stress in soybeans

NanoUPLC-MSE proteomic data assessment of soybean seeds using the Uniprot database

Genome-wide identification and expression analyses of the LEA protein gene family in tea plant reveal their involvement in seed development and abiotic stress responses

Contact Info

Product

Resources

About