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Eucalyptus urograndis stem proteome is responsive to short-term cold stress.

Leonardi Gde A, Carlos NA, Mazzafera P, Balbuena TS - Genet. Mol. Biol. (2015)

Bottom Line: Using two-dimensional gel electrophoresis coupled to high-resolution mass spectrometry-based protein identification, 12 proteins were found to be differentially regulated and successfully identified after stringent database searches against a protein database from a closely related species (Eucalyptus grandis).The identification of these proteins indicated that the E. urograndis stem proteome responded quickly to low temperature, mostly by down-regulating specific proteins involved in energy metabolism, protein synthesis and signaling.The results of this study represent the first step in understanding the molecular and biochemical responses of E. urograndis to thermal stress.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias, Universidade Estadual Paulista "Júlio de Mesquita Filho", Jaboticabal, SP, Brazil.

ABSTRACT
Eucalyptus urograndis is a hybrid eucalyptus of major economic importance to the Brazilian pulp and paper industry. Although widely used in forest nurseries around the country, little is known about the biochemical changes imposed by environmental stress in this species. In this study, we evaluated the changes in the stem proteome after short-term stimulation by exposure to low temperature. Using two-dimensional gel electrophoresis coupled to high-resolution mass spectrometry-based protein identification, 12 proteins were found to be differentially regulated and successfully identified after stringent database searches against a protein database from a closely related species (Eucalyptus grandis). The identification of these proteins indicated that the E. urograndis stem proteome responded quickly to low temperature, mostly by down-regulating specific proteins involved in energy metabolism, protein synthesis and signaling. The results of this study represent the first step in understanding the molecular and biochemical responses of E. urograndis to thermal stress.

No MeSH data available.


Related in: MedlinePlus

Structure and molecular phylogeny analysis for the E. urograndis protein Eucgr.K02072.1 (A) ScanProsite output. Predicted myb-like domain profile extends from amino acid residue 98 through residue 163. (B) Neighbor-joining tree branch containing the E. urograndis protein Eucgr.K02072.1 and the closely-related E. grandis sequences.
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f02: Structure and molecular phylogeny analysis for the E. urograndis protein Eucgr.K02072.1 (A) ScanProsite output. Predicted myb-like domain profile extends from amino acid residue 98 through residue 163. (B) Neighbor-joining tree branch containing the E. urograndis protein Eucgr.K02072.1 and the closely-related E. grandis sequences.

Mentions: Low temperature stress also decreased the expression of proteins involved in gene transcription, such as the protein Eucgr.K02072.1, described as a transcription factor GT-2 containing a trihelix DNA-binding/SANT domain (spot 87). InterPro and Prosite prediction analyses revealed the presence of a myb-like domain from residue 98 through residue 163 of this differentially regulated protein (Figure 2A). A novel myb transcription factor was recently reported to enhance cold tolerance in Arabidopsis (Su et al., 2014). Up-regulation of myb-related transcripts/proteins upon cold stress has also been identified in other plants, such as Anthurium sp. (Tian et al., 2013) and Lilium lancifolium (Wang et al., 2014). Although not extensively described, a correlation between myb proteins and cold stress has already been reported for Eucalyptus. Keller et al. (2009) identified myb-like proteins as the most abundant transcription factors in E. gunnii leaves exposed to cold stress. Large-scale transcript analysis of E. grandis, E. globulus and E. urophylla xylem tissue indicated a differential expression of myb-like proteins across these Eucalyptus species (Salazar et al., 2013). In the present work, the protein Eucgr.K02072.1 identified in young E. urograndis stems was down-regulated after short-term cold exposure.


Eucalyptus urograndis stem proteome is responsive to short-term cold stress.

Leonardi Gde A, Carlos NA, Mazzafera P, Balbuena TS - Genet. Mol. Biol. (2015)

Structure and molecular phylogeny analysis for the E. urograndis protein Eucgr.K02072.1 (A) ScanProsite output. Predicted myb-like domain profile extends from amino acid residue 98 through residue 163. (B) Neighbor-joining tree branch containing the E. urograndis protein Eucgr.K02072.1 and the closely-related E. grandis sequences.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4530643&req=5

f02: Structure and molecular phylogeny analysis for the E. urograndis protein Eucgr.K02072.1 (A) ScanProsite output. Predicted myb-like domain profile extends from amino acid residue 98 through residue 163. (B) Neighbor-joining tree branch containing the E. urograndis protein Eucgr.K02072.1 and the closely-related E. grandis sequences.
Mentions: Low temperature stress also decreased the expression of proteins involved in gene transcription, such as the protein Eucgr.K02072.1, described as a transcription factor GT-2 containing a trihelix DNA-binding/SANT domain (spot 87). InterPro and Prosite prediction analyses revealed the presence of a myb-like domain from residue 98 through residue 163 of this differentially regulated protein (Figure 2A). A novel myb transcription factor was recently reported to enhance cold tolerance in Arabidopsis (Su et al., 2014). Up-regulation of myb-related transcripts/proteins upon cold stress has also been identified in other plants, such as Anthurium sp. (Tian et al., 2013) and Lilium lancifolium (Wang et al., 2014). Although not extensively described, a correlation between myb proteins and cold stress has already been reported for Eucalyptus. Keller et al. (2009) identified myb-like proteins as the most abundant transcription factors in E. gunnii leaves exposed to cold stress. Large-scale transcript analysis of E. grandis, E. globulus and E. urophylla xylem tissue indicated a differential expression of myb-like proteins across these Eucalyptus species (Salazar et al., 2013). In the present work, the protein Eucgr.K02072.1 identified in young E. urograndis stems was down-regulated after short-term cold exposure.

Bottom Line: Using two-dimensional gel electrophoresis coupled to high-resolution mass spectrometry-based protein identification, 12 proteins were found to be differentially regulated and successfully identified after stringent database searches against a protein database from a closely related species (Eucalyptus grandis).The identification of these proteins indicated that the E. urograndis stem proteome responded quickly to low temperature, mostly by down-regulating specific proteins involved in energy metabolism, protein synthesis and signaling.The results of this study represent the first step in understanding the molecular and biochemical responses of E. urograndis to thermal stress.

View Article: PubMed Central - PubMed

Affiliation: Departamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias, Universidade Estadual Paulista "Júlio de Mesquita Filho", Jaboticabal, SP, Brazil.

ABSTRACT
Eucalyptus urograndis is a hybrid eucalyptus of major economic importance to the Brazilian pulp and paper industry. Although widely used in forest nurseries around the country, little is known about the biochemical changes imposed by environmental stress in this species. In this study, we evaluated the changes in the stem proteome after short-term stimulation by exposure to low temperature. Using two-dimensional gel electrophoresis coupled to high-resolution mass spectrometry-based protein identification, 12 proteins were found to be differentially regulated and successfully identified after stringent database searches against a protein database from a closely related species (Eucalyptus grandis). The identification of these proteins indicated that the E. urograndis stem proteome responded quickly to low temperature, mostly by down-regulating specific proteins involved in energy metabolism, protein synthesis and signaling. The results of this study represent the first step in understanding the molecular and biochemical responses of E. urograndis to thermal stress.

No MeSH data available.


Related in: MedlinePlus