Abstract
Shewanella putrefaciens is a specific spoilage bacterium for fish during cold storage. To better understand the molecular mechanisms of cold stress adaptation of S. putrefaciens, tandem mass tag- (TMT-) based quantitative proteomic analysis was performed to detect the effects of cold stress on protein expression profiles in S. putrefaciens which had been cultivated at 4°C and 30°C, respectively. A total of 266670 peptide spectrum matching numbers were quantified proteins after data analysis. Of the 2292 proteins quantitatively analyzed, a total of 274 were found to be differentially expressed (DE) under cold stress compared with the nonstress control. By integrating the results of Kyoto Encyclopedia of Genes and Genomes (KEGG) analyses, 9 common KEGG terms were found notable for the cold-responsive proteins. Generally, the DE proteins involved in carbohydrate, amino acid, and fatty acid biosynthesis and metabolism were significantly upregulated, leading to a specific energy conservation survival mode. The DE proteins related to DNA repair, transcription, and translation were upregulated, implicating change of gene expression and more protein biosynthesis needed in response to cold stress.
Highlights
Fresh fish is very perishable due to endogenous enzymes and microbial activities, which can result in large economic losses [1]
With the stability of the secondary structure of DNA and RNA, in the case of reduced transcription and translation efficiency and low protein folding efficiency, RPs need to adapt to cold stress in order to function normally [41]
Several factors are upregulated under low temperature stress, such as proteins involved in translation, chaperones involved in protein folding, and proteins involved in transcription found in Streptococcus putrefaciens. is shows that S. putrefaciens entered a stabilized phase, which is distinct from the state upon cold shock [15]
Summary
Fresh fish is very perishable due to endogenous enzymes and microbial activities, which can result in large economic losses [1]. S. putrefaciens has been reported to be able to use electron acceptors, such as TMAO, instead of oxygen to survive under oxygen or hypoxia conditions. It can produce proteolytic and lipolytic enzymes broken down proteins and produce various flavour defects to lower the fish quality [7]. Proteomics can provide advanced information on microbial metabolism and mechanisms of adaption to the cold stress environment, and this knowledge could be useful to reveal the cold-adaptation mechanisms in S. putrefaciens. To provide insight into potential mechanisms underlying the ability of S. putrefaciens to grow at a temperature of 4°C, we investigated the whole proteome response of S. putrefaciens exposed to cold stress using mass spectrometry
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