Full TGIF Record # 134554
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Web URL(s):http://turf.rutgers.edu/research/abstracts/symposium2008.pdf
    Last checked: 11/05/2015
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Publication Type:
i
Report
Content Type:Abstract or Summary only
Author(s):Xu, Chenping; Huang, Bingru
Author Affiliation:Department of Plant Biology and Pathology, Rutgers University, New Brunswick, New Jersey
Title:Identification of heat-responsive proteins in two Agrostis species contrasting in heat tolerance using two-dimensional electropheresis and mass spectrometry
Section:Poster presentations
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Meeting Info.:New Brunswick, NJ: January 10-11, 2008
Source:Proceedings of the Seventeenth Annual Rutgers TurfgrassSymposium. 2008, p. 57.
Publishing Information:New Brunswick, NJ: Center for Turfgrass Science, Cook College, Rutgers, The State University of New Jersey
# of Pages:1
Keywords:TIC Keywords: Proteins; Agrostis scabra; Agrostis stolonifera; Heat resistance; Protein metabolism; Temperatures; Electrophoresis; Mass spectrometry
Abstract/Contents:"Protein metabolism plays key role in plant adaptation to heat stress. The objective of this study was to identify novel, up-regulated, or down-regulated proteins associated with heat tolerance in two Agrostis grass species contrasting in heat tolerance. Thermal A. scabra adapted to geothermal soils to temperatures up to 45°C and creeping bentgrass (A. stolonifera) adapted to cool climatic regions were examined. Plants were grown in growth chambers with different temperatures (20°C - optimum control, 30°C - moderate heat stress, and 40°C - severe heat stress). Roots were harvested for proteomic analysis at 2 and 10 days after treatment. The root proteins were spearated by two-dimensional polyacrylamide gel electrophoresis, and identified by mass spectrometry. More than 300 protein spots were reproducibly resolved and detected on each gel. Statistical analysis showed that more than 70 proteins were differentially expressed in roots exposed to 30°C and 40°C compared to those grown at 20°C and between thermal A. scabra and A. stolonifera under heat stress. The number of proteins altered in their expression by heat stress increased with increasing temperatures or stress severity. MALDI-TOF mass spectrometry revealed that proteins with diverse functions were induced or degraded under heat stress, including those involved in stress defense, carbon and energy metabolism."
Language:English
References:0
Note:This item is an abstract only!
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Xu, C., and B. Huang. 2008. Identification of heat-responsive proteins in two Agrostis species contrasting in heat tolerance using two-dimensional electropheresis and mass spectrometry. Proc. Annu. Rutgers Turfgrass Symp. p. 57.
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http://turf.rutgers.edu/research/abstracts/symposium2008.pdf
    Last checked: 11/05/2015
    Requires: PDF Reader
    Notes: Item is within a single large file
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MSU catalog number: SB 433 .R88
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