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Characterization of ClpS2, an essential adaptor protein for the cyanobacterium Synechococcus elongatus

The adaptor protein ClpS associates to the Clp protease and promotes degradation of N-end rule substrates in eubacteria and in algal/plant chloroplasts. Cyanobacteria are unusual in having two distinct ClpS paralogs. Although ClpSl is typical of bacterial ClpS, ClpS2 differs in crucial ways. ClpS2 i...

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Hauptverfasser: Tryggvesson, Anders (VerfasserIn) , Ståhlberg, Frida M. (VerfasserIn) , Töpel, Mats (VerfasserIn) , Tanabe, Noriaki (VerfasserIn) , Mogk, Axel (VerfasserIn) , Clarke, Adrian K. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 24 November 2
In: FEBS letters
Year: 2015, Jahrgang: 589, Heft: 24, part B, Pages: 4039-4046
ISSN:1873-3468
DOI:10.1016/j.febslet.2015.11.026
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2015.11.026
Verlag, lizenzpflichtig, Volltext: https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2015.11.026
Volltext
Verfasserangaben:Anders Tryggvesson, Frida M. Ståhlberg, Mats Töpel, Noriaki Tanabe, Axel Mogk, Adrian K. Clarke
Beschreibung
Zusammenfassung:The adaptor protein ClpS associates to the Clp protease and promotes degradation of N-end rule substrates in eubacteria and in algal/plant chloroplasts. Cyanobacteria are unusual in having two distinct ClpS paralogs. Although ClpSl is typical of bacterial ClpS, ClpS2 differs in crucial ways. ClpS2 in Synechococcus elongatus is a relatively low-abundant, soluble protein essential for phototrophic growth. Like ClpSl, ClpS2 binds to the ClpCP3/R protease to block α-casein degradation and promote that of N-end rule substrates in vitro. However, their substrate specificity differs, with ClpSl recognizing destabilizing Phe and Tyr residues at the substrate N-terminus whereas ClpS2 recognizes Leu. Overall, ClpS2 appears to have independently evolved in cyanobacteria to degrade a particular group of proteins, whose turnover is vital for cell viability.
Beschreibung:Gesehen am 06.07.2020
Beschreibung:Online Resource
ISSN:1873-3468
DOI:10.1016/j.febslet.2015.11.026

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