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Subcellular proteomic characterization of the high-temperature stress response of the cyanobacterium Spirulina platensis.

Hongsthong A, Sirijuntarut M, Yutthanasirikul R, Senachak J, Kurdrid P, Cheevadhanarak S, Tanticharoen M - Proteome Sci (2009)

Bottom Line: The clustering of all differentially expressed proteins in the three cellular compartments showed: (i) the majority of the proteins in all fractions were sustained tolerance proteins, suggesting the roles of these proteins in the tolerance to high temperature stress, (ii) the level of resistance proteins in the photosynthetic membrane was 2-fold higher than the level in two other fractions, correlating with the rapid inactivation of the photosynthetic system in response to high temperature.Subcellular communication among the three cellular compartments via protein-protein interactions was clearly shown by the PPI network analysis.Furthermore, this analysis also showed a connection between temperature stress and nitrogen and ammonia assimilation.

View Article: PubMed Central - HTML - PubMed

Affiliation: National Center for Genetic Engineering and Biotechnology, Thakham, Bangkhuntien, Bangkok, Thailand. apiradee@biotec.or.th

ABSTRACT
The present study examined the changes in protein expression in Spirulina platensis upon exposure to high temperature, with the changes in expression analyzed at the subcellular level. In addition, the transcriptional expression level of some differentially expressed proteins, the expression pattern clustering, and the protein-protein interaction network were analyzed. The results obtained from differential expression analysis revealed up-regulation of proteins involved in two-component response systems, DNA damage and repair systems, molecular chaperones, known stress-related proteins, and proteins involved in other biological processes, such as capsule formation and unsaturated fatty acid biosynthesis. The clustering of all differentially expressed proteins in the three cellular compartments showed: (i) the majority of the proteins in all fractions were sustained tolerance proteins, suggesting the roles of these proteins in the tolerance to high temperature stress, (ii) the level of resistance proteins in the photosynthetic membrane was 2-fold higher than the level in two other fractions, correlating with the rapid inactivation of the photosynthetic system in response to high temperature. Subcellular communication among the three cellular compartments via protein-protein interactions was clearly shown by the PPI network analysis. Furthermore, this analysis also showed a connection between temperature stress and nitrogen and ammonia assimilation.

No MeSH data available.


Related in: MedlinePlus

Pie charts representing percentage of each protein cluster classified by the expression pattern of all significant differentially expressed proteins in the soluble fraction (clusters 9, 17 and 20 are resistance proteins, clusters 7, 12 and 21 are adaptation proteins, clusters 1, 2, 3, 6, 16, 18 and 19 are sustained proteins, and clusters 4, 5, 8, 10, 11, 13, 14, 15, 22 and 23 are undetermined protein trends).
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Figure 12: Pie charts representing percentage of each protein cluster classified by the expression pattern of all significant differentially expressed proteins in the soluble fraction (clusters 9, 17 and 20 are resistance proteins, clusters 7, 12 and 21 are adaptation proteins, clusters 1, 2, 3, 6, 16, 18 and 19 are sustained proteins, and clusters 4, 5, 8, 10, 11, 13, 14, 15, 22 and 23 are undetermined protein trends).

Mentions: The proteins with significantly differential expression in each subcellular fraction were clustered, based on their expression patterns [see fig S6; Additional file 2]. According to Lacerda et al., the expression patterns in response to stress can be classified into three major groups: resistance, adaptation and sustained tolerance [38]. The results shown in Fig. 11, 12 and 13 demonstrate that the majority of proteins in every subcellular fraction belong to the sustained tolerance expression pattern. If all differentially expressed proteins are set as 100%, the percentages of the resistance, adaptation and sustained tolerance groups are: (i) 7%, 3% and 46% in the PM fraction, (ii) 9%, 10%, 46% in the soluble fraction and (iii) 18%, 12% and 58% in the TM fraction, respectively. It should be noted that some patterns do not fit into any categories, and these patterns were mostly found in the PM fraction. Moreover, the plasma membrane, where the environmental changes are first encountered, is the only site where the resistance proteins are present at a significantly higher level than the adaptation proteins.


Subcellular proteomic characterization of the high-temperature stress response of the cyanobacterium Spirulina platensis.

Hongsthong A, Sirijuntarut M, Yutthanasirikul R, Senachak J, Kurdrid P, Cheevadhanarak S, Tanticharoen M - Proteome Sci (2009)

Pie charts representing percentage of each protein cluster classified by the expression pattern of all significant differentially expressed proteins in the soluble fraction (clusters 9, 17 and 20 are resistance proteins, clusters 7, 12 and 21 are adaptation proteins, clusters 1, 2, 3, 6, 16, 18 and 19 are sustained proteins, and clusters 4, 5, 8, 10, 11, 13, 14, 15, 22 and 23 are undetermined protein trends).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2743650&req=5

Figure 12: Pie charts representing percentage of each protein cluster classified by the expression pattern of all significant differentially expressed proteins in the soluble fraction (clusters 9, 17 and 20 are resistance proteins, clusters 7, 12 and 21 are adaptation proteins, clusters 1, 2, 3, 6, 16, 18 and 19 are sustained proteins, and clusters 4, 5, 8, 10, 11, 13, 14, 15, 22 and 23 are undetermined protein trends).
Mentions: The proteins with significantly differential expression in each subcellular fraction were clustered, based on their expression patterns [see fig S6; Additional file 2]. According to Lacerda et al., the expression patterns in response to stress can be classified into three major groups: resistance, adaptation and sustained tolerance [38]. The results shown in Fig. 11, 12 and 13 demonstrate that the majority of proteins in every subcellular fraction belong to the sustained tolerance expression pattern. If all differentially expressed proteins are set as 100%, the percentages of the resistance, adaptation and sustained tolerance groups are: (i) 7%, 3% and 46% in the PM fraction, (ii) 9%, 10%, 46% in the soluble fraction and (iii) 18%, 12% and 58% in the TM fraction, respectively. It should be noted that some patterns do not fit into any categories, and these patterns were mostly found in the PM fraction. Moreover, the plasma membrane, where the environmental changes are first encountered, is the only site where the resistance proteins are present at a significantly higher level than the adaptation proteins.

Bottom Line: The clustering of all differentially expressed proteins in the three cellular compartments showed: (i) the majority of the proteins in all fractions were sustained tolerance proteins, suggesting the roles of these proteins in the tolerance to high temperature stress, (ii) the level of resistance proteins in the photosynthetic membrane was 2-fold higher than the level in two other fractions, correlating with the rapid inactivation of the photosynthetic system in response to high temperature.Subcellular communication among the three cellular compartments via protein-protein interactions was clearly shown by the PPI network analysis.Furthermore, this analysis also showed a connection between temperature stress and nitrogen and ammonia assimilation.

View Article: PubMed Central - HTML - PubMed

Affiliation: National Center for Genetic Engineering and Biotechnology, Thakham, Bangkhuntien, Bangkok, Thailand. apiradee@biotec.or.th

ABSTRACT
The present study examined the changes in protein expression in Spirulina platensis upon exposure to high temperature, with the changes in expression analyzed at the subcellular level. In addition, the transcriptional expression level of some differentially expressed proteins, the expression pattern clustering, and the protein-protein interaction network were analyzed. The results obtained from differential expression analysis revealed up-regulation of proteins involved in two-component response systems, DNA damage and repair systems, molecular chaperones, known stress-related proteins, and proteins involved in other biological processes, such as capsule formation and unsaturated fatty acid biosynthesis. The clustering of all differentially expressed proteins in the three cellular compartments showed: (i) the majority of the proteins in all fractions were sustained tolerance proteins, suggesting the roles of these proteins in the tolerance to high temperature stress, (ii) the level of resistance proteins in the photosynthetic membrane was 2-fold higher than the level in two other fractions, correlating with the rapid inactivation of the photosynthetic system in response to high temperature. Subcellular communication among the three cellular compartments via protein-protein interactions was clearly shown by the PPI network analysis. Furthermore, this analysis also showed a connection between temperature stress and nitrogen and ammonia assimilation.

No MeSH data available.


Related in: MedlinePlus