The N termini of Brassica and tung omega-3 fatty acid desaturases mediate proteasome-dependent protein degradation in plant cells

Khuu, Nicholas; Gidda, Satinder K.; Shockey, Jay; Dyer, John M.; Mullen, Robert T.

doi:10.4161/psb.6.3.14522

Cited by 10 publications

(6 citation statements)

References 18 publications

(30 reference statements)

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“…It appears that protein degradation is a preferred level on which temperature imposes the effect. The amino acid segments accounting for the thermal instability of several FADs have been mapped, including the C-terminal region of FAD8 from Arabidopsis (Matsuda et al, 2005), the N-terminal and 241-334 regions of FAD2-1A from soybean (Glycine max) (Tang et al, 2005), and the N-terminal region of FAD3 from Brassica napus (Khuu et al, 2011). In addition, GmFAD2-1A and -1B have also been observed to undergo Ser185 phosphorylation that may impair their activities (Tang et al, 2005).…”

Section: Fatty Acid Desaturasesmentioning

confidence: 99%

Plant Unsaturated Fatty Acids: Biosynthesis and Regulation

et al. 2020

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In most plants, major unsaturated fatty acids (UFAs) are three C18 species, namely, oleic (18:1), linoleic (18:2), and α-linolenic (18:3) acids. These simple compounds play multiple crucial roles in planta and are also important economic traits of oil crops. The enzymatic steps of C18 UFA biosynthesis have been well established. However, the associated FA/lipid trafficking between the plastid and the endoplasmic reticulum remains largely unclear, as does the regulation of the expression and activities of the involved enzymes. In this review, we will revisit the biosynthesis of C18 UFAs with an emphasis on the trafficking, and present an overview of the key enzymes and their regulation. Of particular interest is the emerging regulatory network composed of transcriptional factors and upstream signaling pathways. The review thereby provides the promise of using physical, biochemical and/or genetic means to manipulate FA composition and increase oil yield in crop improvement.

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Section: Fatty Acid Desaturasesmentioning

confidence: 99%

Plant Unsaturated Fatty Acids: Biosynthesis and Regulation

et al. 2020

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“…In addition, the N-terminus of FAD2-1 and FAD3 was shown to be important in the temperature-dependent turnover of proteins. The FAD2 and FAD3 proteins were thus less stable and hence, less abundant at high temperatures ( Khuu et al, 2011 ). Domain-swapping and mutagenesis experiments revealed that each protein contained a degradation signal in its N-terminus, and the PEST-like sequence within this region was largely responsible for the rates of protein turnover.…”

Section: Regulation Of Fad2 Genementioning

confidence: 99%

The FAD2 Gene in Plants: Occurrence, Regulation, and Role

et al. 2017

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Vegetable oils rich in oleic acid are more desirable than oils rich in polyunsaturated and saturated fatty acids. The biological switch of oleic acid to linoleic acid is facilitated by fatty acid desaturase 2 enzyme that is further classified into FAD2-1, FAD2-2, FAD2-3, and FAD2-4. The genes coding these enzymes have high sequence similarity, but differ mostly in their expression patterns. The seed-type FAD2 genes had evolved independently after segregation by duplication from constitutively expressed FAD2 genes. Temperature, light and wounding effectively regulate FAD2 expression in plants. FAD2 genes are expressed differently in different tissues of the plant, and the over-expression of FAD2 modifies physiological and vegetative characteristics. The activity of FAD2 leads to an increase in the content of dienoic fatty acids, and hence increases the resistance toward cold and salt stress. The thorough study of the FAD2 gene is important for understanding the expression, regulation and mechanism that will help in improving the quality of oil and stress resistance in plants.

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“…In particular, heterologous expression studies in yeast (Saccharomyces cerevisiae) have demonstrated that FAD2 and FAD3 proteins are less stable and, therefore, less abundant at elevated temperatures (Dyer et al, 2001;Sánchez-García et al, 2004;Tang et al, 2005;O'Quin et al, 2010;Khuu et al, 2011). Furthermore, studies have shown that the effect of temperature on FAD2 and FAD3 protein abundance is determined by a combination of cis-acting degradation signals and the ubiquitin-proteasome pathway (Tang et al, 2005;O'Quin et al, 2010).…”

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confidence: 99%