Protease activities in the chloroplast capable of cleaving an LHCII N-terminal peptide

Abstract

Two protease activities of pea chloroplasts, one located in the stroma and the other associated to the thylakoid membrane, are described. Both proteases catalyse the endo-proteolytic cleavage of a peptide corresponding to the N-terminal loop and the first turn in helix-B of light-harvesting complex II (Lhcb1 from pea). The stromal protease cleaves preferentially on the carboxy-side of glutamic acid residues. Inhibitor studies indicate that this protease is a serine-type protease. The protease was partially purified and could be correlated to a 95-kDa polypeptide band on SDS-polyacrylamide gels. The 95 kDa protein was partially sequenced and showed similarity to an to an 'unknown protein' from A. thaliana (in the NCBI public database) as well as to a glutamyl endopeptidase purified from crude extract of cucumber leaves. It is concluded that the stromal protease is a chloroplast glutamyl endopeptidase (cGEP). The protease localized in the thylakoid membrane, cleaved the peptide at only one site, close to its N terminus. The activity of the thylakoid-associated protease was found to be drastically increased in the presence of the reducing agent 1,4-dithiothreitol. Inhibitor studies suggest that this protease is a cysteine- or serine-type protease. The possible roles of these proteases in the regulation of photosynthetic electron transport and in the chloroplast homeostasis are discussed

Published in

Physiologia Plantarum
2005, volume: 123, number: 1, pages: 21-29
Publisher: BLACKWELL MUNKSGAARD

SLU Authors

• Larsson, Håkan

  • Department of Plant Biology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Bioenergy
Agricultural Science
Renewable Bioenergy Research

Publication identifier

• DOI: https://doi.org/10.1111/j.1399-3054.2005.00441.x

Permanent link to this page (URI)

https://res.slu.se/id/publ/8504