ConCysFind: a pipeline tool to predict conserved amino acids of protein sequences across the plant kingdom

Moore, Marten; Wesemann, Corinna; Gossmann, Nikolaj; Sahm, Arne; Kruger, Jan Walters; Sczyrba, Alexander; Dietz, Karl‐Josef

doi:10.1186/s12859-020-03749-2

Cited by 4 publications

(2 citation statements)

References 33 publications

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“…Amino acid residues available for post-translational modifications are typically located in functional domains and a conserved sequence environment, as they confer some evolutionary constraints/stability on residues that are modified [48, 49]. We hypothesized that S-acylated cysteine residues in CAPN5 were likely conserved.…”

Section: Resultsmentioning

confidence: 99%

S-Acylation Regulates the Membrane Association and Activity of Calpain-5

Gál

Bondada

Mashburn

et al. 2022

Preprint

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Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 domains often have affinity to lipids, mediating membrane association. We recently reported that the C2 domain of CAPN5 was essential for its membrane association and the activation of its autolytic activity. However, despite the removal of the C2 domain by autolysis, the N-terminal fragment of CAPN5 remained membrane associated. S-acylation, also referred to as S-palmitoylation, is a reversible post-translational lipid modification of cysteine residues that promotes membrane association of soluble proteins. In the present study several S-acylated cysteine residues were identified in CAPN5 with the acyl-PEG exchange method. Data reported here demonstrate that CAPN5 is S-acylated on up to three cysteine residues including Cys-4 and Cys-512, and likely Cys-507. The D589N mutation in a potential calcium binding loop within the C2 domain interfered with the S-acylation of CAPN5, likely preventing initial membrane association. Mutating specific cysteine residues of CAPN5 interfered with both its membrane association and the activation of CAPN5 autolysis. Taken together, our results suggest that the S-acylation of CAPN5 is critical for its membrane localization which appears to favor its enzymatic activity.

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Section: Resultsmentioning

confidence: 99%

S-Acylation Regulates the Membrane Association and Activity of Calpain-5

Gál

Bondada

Mashburn

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…The difficulty of predicting S-acylated cysteine residues in human proteins is due in part to the large number of protein S-acyltransferases in the human proteome [46,47]. Amino acid residues available for post-translational modifications are typically located in functional domains and a conserved sequence environment, as they confer some evolutionary constraints/stability on residues that are modified [48,49]. We hypothesized that S-acylated cysteine residues in CAPN5 were likely conserved.…”

Section: Prediction Of Sites Of S-acylation Within Capn5 Replacing In...mentioning

confidence: 99%