Premium
Identification of the N‐termini of NADPH : protochlorophyllide oxidoreductase A and B from barley etioplasts ( Hordeum vulgare L.)
Author(s) -
Plöscher Matthias,
Granvogl Bernhard,
Reisinger Veronika,
Eichacker Lutz A.
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06850.x
Subject(s) - protochlorophyllide , hordeum vulgare , biochemistry , signal peptide , oxidoreductase , peptide , pentapeptide repeat , biology , peptide sequence , chemistry , enzyme , gene , botany , poaceae
The N‐termini of the NADPH : protochlorophyllide oxidoreductase (POR) proteins A and B from barley and POR from pea were determined by acetylation of the proteins and selective isolation of the N‐terminal peptides for mass spectrometry de novo sequence analysis. We show that the cleavage sites between the transit peptides and the three mature POR proteins are homologous. The N‐terminus in PORA is V48, that in PORB is A61, and that in POR from pea is E64. For the PORB protein, two additional N‐termini were identified as A62 and A63, with decreased signal intensity of the corresponding N‐terminal peptides. The results show that the transit peptide of PORA is considerably shorter than previously reported and predicted by ChloroP. A pentapeptide motif that has been characterized as responsible for binding of protochlorophyllide to the transit peptide of PORA [Reinbothe C, Pollmann S, Phetsarath‐Faure P, Quigley F, Weisbeek P & Reinbothe S (2008) Plant Physiol 148 , 694–703] is shown here to be part of the mature PORA protein.