N‐degron specificity of chloroplast ClpS1 in plants
In: FEBS Letters, Jg. 593 (2019-04-20), S. 962-970
Online
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Zugriff:
The prokaryotic N-degron pathway depends on the Clp chaperone-protease system and the ClpS adaptor for recognition of N-degron bearing substrates. Plant chloroplasts contain a diversified Clp protease, including the ClpS homolog ClpS1. Several candidate ClpS1 substrates have been identified, but the N-degron specificity is unclear. Here, we employed in vitro ClpS1 affinity assays using eight N-degron green fluorescence protein reporters containing either F, Y, L, W, I, or R in the N-terminal position. This demonstrated that ClpS1 has a restricted N-degron specificity, recognizing proteins bearing an N-terminal F or W, only weakly recognizing L, but not recognizing Y or I. This affinity is dependent on two conserved residues in the ClpS1 binding pocket and is sensitive to FR dipeptide competition, suggesting a unique chloroplast N-degron pathway.
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N‐degron specificity of chloroplast ClpS1 in plants
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Autor/in / Beteiligte Person: | Dougan, David A. ; Klaas J. van Wijk ; Montandon, Cyrille |
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Zeitschrift: | FEBS Letters, Jg. 593 (2019-04-20), S. 962-970 |
Veröffentlichung: | Wiley, 2019 |
Medientyp: | unknown |
ISSN: | 1873-3468 (print) ; 0014-5793 (print) |
DOI: | 10.1002/1873-3468.13378 |
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