PMID- 20113435
OWN - NLM
STAT- MEDLINE
DCOM- 20100914
LR  - 20100625
IS  - 1399-3054 (Electronic)
IS  - 0031-9317 (Linking)
VI  - 139
IP  - 2
DP  - 2010 Jun 1
TI  - Differential proteomic response to heat stress in thermal Agrostis scabra and 
      heat-sensitive Agrostis stolonifera.
PG  - 192-204
LID - 10.1111/j.1399-3054.2010.01357.x [doi]
AB  - Knowledge of heat-responsive proteins is critical for further understanding of 
      the molecular mechanisms of heat tolerance. The objective of this study was to 
      compare proteins differentially expressed in two C(3) grass species contrasting 
      in heat tolerance, heat-tolerant thermal Agrostis scabra and heat-sensitive 
      Agrostis stolonifera L., and to identify heat-responsive proteins for short- and 
      long-term responses. Plants were exposed to 20/15 degrees C (day/night, control) 
      or 40/35 degrees C (day/night, heat stress) in growth chambers. Leaves were 
      harvested at 2 and 10 days after temperature treatment. Proteins were extracted 
      and separated by fluorescence difference gel electrophoresis (DIGE). Thermal A. 
      scabra had superior heat tolerance than A. stolonifera, as indicated by the 
      maintenance of higher chlorophyll content and photochemical efficiency under heat 
      stress. The two-dimensional difference electrophoresis detected 68 
      heat-responsive proteins in the two species. Thermal A. scabra had more protein 
      spots either down- or up-regulated at 2 days of heat stress, but fewer protein 
      spots were altered at 10 days of heat stress compared with A. stolonifera. Many 
      protein spots exhibited transient down-regulation in thermal A. scabra (only at 2 
      days of heat treatment), whereas down-regulation of many proteins was also found 
      at 10 days of heat treatment in A. stolonifera, which suggested that protein 
      metabolism in thermal A. scabra might acclimate to heat stress more rapidly than 
      those in A. stolonifera. The sequences of 56 differentially expressed protein 
      spots were identified using mass spectrometry. The results suggest that the 
      maintenance or less severe down-regulation of proteins during long-term (10 days) 
      heat stress may contribute to the superior heat tolerance in thermal A. scabra, 
      including those involved in photosynthesis [RuBisCo, RuBisCo activase, 
      chloroplastic glyceraldehydes-3-phosphate dehydrogenase (GAPDH), chloroplastic 
      aldolase, oxygen-evolving complex, photosystem I subunits], dark respiration 
      (cytosolic GAPDH, cytoplasmic aldolase, malate dehydrogenase, hydroxypyruvate 
      reductase, sedoheptulose-1,7-bisphosphatase), photorespiration [(hydroxypyruvate 
      reductase, alanine aminotransferase (AlaAT), hydroxymethyltransferase (SHMT), 
      glycine decarboxylase (GDC)], as well as heat and oxidative stress protection 
      [heat shock cognate (HSC) 70 and FtsH-like protein].
FAU - Xu, Chenping
AU  - Xu C
AD  - Department of Plant Biology and Pathology, Rutgers University, New Brunswick, NJ 
      08901, USA.
FAU - Huang, Bingru
AU  - Huang B
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100125
PL  - Denmark
TA  - Physiol Plant
JT  - Physiologia plantarum
JID - 1256322
RN  - 0 (Plant Proteins)
RN  - 0 (Proteome)
RN  - 1406-65-1 (Chlorophyll)
SB  - IM
MH  - Agrostis/metabolism/*physiology
MH  - Chlorophyll/analysis
MH  - Heat-Shock Response
MH  - *Hot Temperature
MH  - Plant Leaves/metabolism/physiology
MH  - Plant Proteins/*metabolism
MH  - Proteome/*metabolism
MH  - Stress, Physiological
EDAT- 2010/02/02 06:00
MHDA- 2010/09/15 06:00
CRDT- 2010/02/02 06:00
PHST- 2010/02/02 06:00 [entrez]
PHST- 2010/02/02 06:00 [pubmed]
PHST- 2010/09/15 06:00 [medline]
AID - PPL1357 [pii]
AID - 10.1111/j.1399-3054.2010.01357.x [doi]
PST - ppublish
SO  - Physiol Plant. 2010 Jun 1;139(2):192-204. doi: 10.1111/j.1399-3054.2010.01357.x. 
      Epub 2010 Jan 25.