Proteomics

Dataset Information

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Aggregated protein of heat-treated GmDnj1 mutant Orbitrap LC-MSMS


ABSTRACT: Gmdnj1-knockout mutants had diminished growth in normal conditions, and when under heat stress, exhibited more severe browning, reduced chlorophyll contents, higher reactive oxygen species (ROS) contents, and higher induction of heat stress-responsive transcription factors and ROS-scavenging enzyme-encoding genes. Knocking out a major HSP40 may lead to the impairment of the protein refolding system, and in turn lead to a change in the aggregated protein profile. Therefore, the aggregated protein profiles of the Gmdnj1 mutant lines were compared against that of the wild type Williams 82 under both untreated and heat-treated conditions.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Glycine Max

TISSUE(S): Root, Leaf

SUBMITTER: Kwan Pok Li  

LAB HEAD: Hon-Ming Lam

PROVIDER: PXD019799 | Pride | 2021-09-09

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
A_20200330.raw Raw
B_20200330.raw Raw
C_20200330.raw Raw
D_20200330.raw Raw
E_20200330.raw Raw
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Publications

GmDNJ1, a type-I heat shock protein 40 (HSP40), is responsible for both Growth and heat tolerance in soybean.

Li Kwan-Pok KP   Wong Cheuk-Hon CH   Cheng Chun-Chiu CC   Cheng Sau-Shan SS   Li Man-Wah MW   Mansveld Sandra S   Bergsma Alex A   Huang Tengfang T   van Eijk Michiel J T MJT   Lam Hon-Ming HM  

Plant direct 20210125 1


Global warming poses severe threats to agricultural production, including soybean. One of the major mechanisms for organisms to combat heat stress is through heat shock proteins (HSPs) that stabilize protein structures at above-optimum temperatures, by assisting in the folding of nascent, misfolded, or unfolded proteins. The HSP40 subgroups, or the J-domain proteins, functions as co-chaperones. They capture proteins that require folding or refolding and pass them on to HSP70 for processing. In t  ...[more]

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