Biochemical characterization of the triticale TsPAP1, a new type of plant prolyl aminopeptidase, and its impact on proline content and flowering time in transgenic Arabidopsis plants

Zdunek‐Zastocka, Edyta; Grabowska, Agnieszka; Branicki, Tomasz; Michniewska, Beata

doi:10.1016/j.plaphy.2017.04.026

Cited by 14 publications

(9 citation statements)

References 42 publications

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“…The accumulation of free proline varies considerably in different plant organs, depending both on the developmental stage of the plant and on the environmental stimuli [12,13]. Proline concentration is usually higher in reproductive organs than in vegetative tissues, and increases significantly in actively dividing cells [12,29,60]. When leaves of control pea plants were analyzed according to their stage of development, the highest concentration of proline was found in the youngest undeveloped A leaves, and it gradually decreased through B leaves towards old C leaves (Figure 2A).…”

Section: Discussionmentioning

confidence: 99%

Proline Concentration and Its Metabolism Are Regulated in a Leaf Age Dependent Manner But Not by Abscisic Acid in Pea Plants Exposed to Cadmium Stress

Zdunek‐Zastocka

Grabowska

Michniewska

et al. 2021

Cells

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The accumulation of proline is one of the defense mechanisms of plants against the harmful effects of adverse environmental conditions; however, when pea plants were treated for 12 h with CdCl2, the proline concentration decreased in the youngest A (not expanded) and B1 (expanded) leaves, and did not change significantly in the B2 (mature, expanded) or C (the oldest) leaves. After 24 h of cadmium (Cd) stress, the proline concentration remained low in A and B1 leaves, while in B2 and C leaves, it increased, and after 48 h, an increase in the proline concentration in the leaves at each stage of development was observed. The role of proline in the different phases of plant response to the Cd treatment is discussed. Changes in proline accumulation corresponded closely with changes in the transcript levels of PsP5CS2, a gene encoding D1-pyrroline-5-carboxylate synthetase involved in proline synthesis, and PsPDH1, a gene encoding proline dehydrogenase engaged in proline degradation. CdCl2 application induced the expression of PsProT1 and PsProT2, genes encoding proline transporters, especially during the first 12 h of treatment in A and B1 leaves. When the time courses of abscisic acid (ABA) and proline accumulation were compared, it was concluded that an increase in the proline concentration in the leaves of Cd-treated pea plants was more related to a decrease in chlorophyll concentration (leaves B2 and C) and an increase in the malondialdehyde level (A and B1 leaves) than with an increase in ABA concentration alone. Exogenous application of ABA (0.5, 5, 50 µM) significantly increased the proline concentration in the A leaves of pea plants only, and was accompanied by an elevated and repressed expression of PsP5CS2 and PsPDH1 in these leaves, respectively. The presented results suggest that under Cd stress, the accumulation of proline in leaves of pea plants may take place independently of the ABA signaling.

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Section: Discussionmentioning

confidence: 99%

Proline Concentration and Its Metabolism Are Regulated in a Leaf Age Dependent Manner But Not by Abscisic Acid in Pea Plants Exposed to Cadmium Stress

Zdunek‐Zastocka

Grabowska

Michniewska

et al. 2021

Cells

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“…PEP/POP from different species have different β-propeller sizes, thus conferring specificity to different sizes of substrates targeting proline residues that are usually resistant to protein cleavage by other peptidases [ 76 , 77 ]. For example, studies on Arabidopsis thaliana , Homo sapiens , and Sus scrofa (porcine) showed that each POP possesses a unique affinity toward different sizes of ligands despite high sequence and structural similarities [ 78 ].…”

Section: Molecular Structure and Biochemistrymentioning

confidence: 99%

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Baharin

Ting

Goh

2022

Plants

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Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several classes of proteases in the MEROPS database based on their catalytic mechanisms. This review focuses on post-proline cleaving enzymes (PPCEs) from different peptidase families, as well as prolyl endoprotease/oligopeptidase (PEP/POP) from the serine peptidase family. To date, most PPCEs studied are of microbial and animal origins. Recently, there have been reports of plant PPCEs. The most common PEP/POP are members of the S9 family that comprise two conserved domains. The substrate-limiting β-propeller domain prevents unwanted digestion, while the α/β hydrolase catalyzes the reaction at the carboxyl-terminal of proline residues. PPCEs display preferences towards the Pro-X bonds for hydrolysis. This level of selectivity is substantial and has benefited the brewing industry, therapeutics for celiac disease by targeting proline-rich substrates, drug targets for human diseases, and proteomics analysis. Protein engineering via mutagenesis has been performed to improve heat resistance, pepsin-resistant capability, specificity, and protein turnover of PPCEs for pharmacological applications. This review aims to synthesize recent structure–function studies of PPCEs from different families of peptidases to provide insights into the molecular mechanism of prolyl cleaving activity. Despite the non-exhaustive list of PPCEs, this is the first comprehensive review to cover the biochemical properties, biological functions, and biotechnological applications of PPCEs from the diverse taxa.

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“…[3][4][5] It has been proven that aminopeptidases are crucial in the processes of germination, meiosis, flowering, aging, stress response and defense in different species. [6][7][8][9][10] Some of the enzymes, crucial for germination process, are synthesized either during embryogenesis (and further activated during imbibition) or just during imbibition. Aminopeptidases with different substrate preferences have been characterized in various plant species, such as barley (Hordeum vulgare), 5 sunflower (Helianthus annuus), 11 triticale (Triticosecale), 12 soybean cotyledons (Glycine max), 13 and Solanum tuberosum tuber.…”

Section: Introductionmentioning

confidence: 99%

Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

2021

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BACKGROUND: Oilseed rape is one of the most important oilseed crops worldwide, crucial in the food and feed industries. Different environment and climatic conditions can influence its sustainable cultivation and crop yield. Aminopeptidases are crucial enzymes in many physiological processes in all organisms, including humans, so it is important to learn their behavior in food and feed sources. This study presents, for the first time, a detailed discussion on the importance of aminopeptidases, during the oilseed rape germination process, under standard and stress conditions. RESULTS: During the germination of oilseed rape under standard conditions, a significant increase in aminopeptidases activity toward N-terminal amino acidsphenylalanine (Phe), alanine (Ala), glycine (Gly), leucine (Leu), proline (Pro), methionine (Met) was observed. The change was substrate specific, with the highest increase being observed for Gly (3.2-fold), followed by Ala (2.9-fold), Pro (2.5-fold), Met (1.5-fold), and Phe (1.3-fold). Generally, N-terminal Phe was preferentially cleaved. Germination under stress conditions, caused by several heavy metal ions (e.g. divalent copper, zinc, cadmium, and lead ions), negatively influenced the plants' growth and quality, but significantly enhanced the expression of genes encoding aminopeptidases (or potentially activated aminopeptidases precursors), which was related to the dramatic increase of their activity.CONCLUSIONS: The activity/concentration of aminopeptidases in plants is adjusted to the needs at each stage of development and stress factors occurrence. The most significant increase of activity toward N-terminal Gly and Pro proved the key role of aminopeptidases in the defense mechanisms, by supplying the plants with osmoprotectants and organic nitrogen. The results provide new concepts of oilseed rape growth and cultivation under different conditions.

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Biochemical characterization of the triticale TsPAP1, a new type of plant prolyl aminopeptidase, and its impact on proline content and flowering time in transgenic Arabidopsis plants

Cited by 14 publications

References 42 publications

Proline Concentration and Its Metabolism Are Regulated in a Leaf Age Dependent Manner But Not by Abscisic Acid in Pea Plants Exposed to Cadmium Stress

Proline Concentration and Its Metabolism Are Regulated in a Leaf Age Dependent Manner But Not by Abscisic Acid in Pea Plants Exposed to Cadmium Stress

Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications

Oilseed rape (Brassica napus): the importance of aminopeptidases in germination under normal and heavy metals stress conditions

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