10.1021/pr501323d.s002
Jin Koh
Jin
Koh
Gang Chen
Gang
Chen
Mi-Jeong Yoo
Mi-Jeong
Yoo
Ning Zhu
Ning
Zhu
Daniel Dufresne
Daniel
Dufresne
John E. Erickson
John E.
Erickson
Hongbo Shao
Hongbo
Shao
Sixue Chen
Sixue
Chen
Comparative Proteomic Analysis
of <i>Brassica
napus</i> in Response to Drought Stress
American Chemical Society
2015
protein expression changes
gene transcription
PTM
protein abundance changes
drought stress
oil seed crop
Comparative Proteomic Analysis
LC
2015-08-07 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Comparative_Proteomic_Analysis_of_i_Brassica_napus_i_in_Response_to_Drought_Stress/2143372
Drought
is one of the most widespread stresses leading to retardation
of plant growth and development. We examined proteome changes of an
important oil seed crop, canola (<i>Brassica napus</i> L.),
under drought stress over a 14-day period. Using iTRAQ LC–MS/MS,
we identified 1976 proteins expressed during drought stress. Among
them, 417 proteins showed significant changes in abundance, and 136,
244, 286, and 213 proteins were differentially expressed in the third,
seventh, 10th, and 14th day of stress, respectively. Functional analysis
indicated that the number of proteins associated with metabolism,
protein folding and degradation, and signaling decreased, while those
related to energy (photosynthesis), protein synthesis, and stress
and defense increased in response to drought stress. The seventh and
10th-day profiles were similar to each other but with more post-translational
modifications (PTMs) at day 10. Interestingly, 181 proteins underwent
PTMs; 49 of them were differentially changed in drought-stressed plants,
and 33 were observed at the 10th day. Comparison of protein expression
changes with those of gene transcription showed a positive correlation
in <i>B. napus</i>, although different patterns between
transcripts and proteins were observed at each time point. Under drought
stress, most protein abundance changes may be attributed to gene transcription,
and PTMs clearly contribute to protein diversity and functions.