PjCLE1 peptide

PjCLE1 peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-RLAOEGONPEHH-OH

H-Arg-Leu-Ala-Hyp-Glu-Gly-Hyp-Asn-Pro-Glu-His-His-OH

12

95.19%

C₅₈H₈₈N₂₀O₂₀

1385.44

Synthetic

Powder

PjCLE1 is an endogenous peptide hormone in the parasitic plant Phtheirospermum japonicum. It was identified through genomic analysis, with 14 PjCLE genes found in the genome, and PjCLE1/Pjv1-77 showing significant expression differences in haustoria compared to non-infecting roots and high expression in laser-dissected mature haustoria. It is processed and activated by the subtilisin-type protease PjSBT1.2.3. When incubated with PjSBT1.2.3-His, the cleavage site within the variable domain of the prodomain was determined, and the fully processed PjCLE1 peptide was generated.
Functionally, PjCLE1 is sufficient to induce protohaustorium formation even in the absence of a host, similar to the haustorium-inducing factor DMBQ. Co-treatment with PjCLE1 and DMBQ leads to more prolific protohaustoria formation. Although shoots are not strictly required for PjCLE1-induced protohaustoria formation, their presence affects the process. Sucrose availability can influence protohaustorium formation under certain conditions, and mineral nutrients generally reduce haustorium formation. PjCLE1 also affects signal transduction, enhancing DMBQ-induced MAPK phosphorylation and inducing the expression of genes related to haustoriogenesis, such as PjYUC3. RNA-Seq analysis indicates a similar transcriptional response to DMBQ treatment, with co-treatment potentiating the effect. Overall, PjCLE1 appears to play a crucial role in regulating haustorium formation in Phtheirospermum japonicum, potentially acting as an internal signal to stimulate additional protohaustorium formation for efficient resource extraction from hosts.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Greifenhagen A, Ruwe H, Zimmer V, Messerschmidt J, Bhukya DPN, Kenea HD, Schaller A, Spallek T. The peptide hormone PjCLE1 stimulates haustorium formation in the parasitic plant Phtheirospermum japonicum. Proc Natl Acad Sci U S A. 2024 Oct 15;121(42):e2414582121. doi: 10.1073/pnas.2414582121. Epub 2024 Oct 9. PMID: 39383005; PMCID: PMC11494319.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.