Sammanfattning

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

Publicerad i

Physiologia Plantarum
2005, Volym: 123, nummer: 1, sidor: 21-29
Utgivare: BLACKWELL MUNKSGAARD

SLU författare

• Larsson, Håkan

  • Institutionen för växtbiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Jordbruksvetenskap
Förnyelsebar bioenergi


Publikationens identifierare

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

Permanent länk till denna sida (URI)

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