Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence

A - Papers appearing in refereed journals

Groten, K., Dutilleul, C., Van Heerden, P. D. R., Vanacker, H., Bernard, S., Finkemeier, I., Dietz, K-J. and Foyer, C. H. 2006. Redox regulation of peroxiredoxin and proteinases by ascorbate and thiols during pea root nodule senescence. FEBS Letters. 580 (5), pp. 1269-1276.

AuthorsGroten, K., Dutilleul, C., Van Heerden, P. D. R., Vanacker, H., Bernard, S., Finkemeier, I., Dietz, K-J. and Foyer, C. H.
Abstract

Redox factors contributing to nodule senescence were studied in pea. The abundance of the nodule cytosolic peroxiredoxin but not the mitochondrial peroxiredoxin protein was modulated by ascorbate. In contrast to redox-active antioxidants such as ascorbate and cytosolic peroxiredoxin that decreased during nodule development, maximal extractable nodule proteinase activity increased progressively as the nodules aged. Cathepsin-like activities were constant throughout development but serine and cysteine proteinase activities increased during senescence. Senescence-induced cysteine proteinase activity was inhibited by cysteine, dithiotreitol, or E-64. Senescence-dependent decreases in redox-active factors, particularly ascorbate and peroxiredoxin favour decreased redox-mediated inactivation of cysteine proteinases. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

KeywordsBiochemistry & Molecular Biology; Biophysics; Cell Biology
Year of Publication2006
JournalFEBS Letters
Journal citation580 (5), pp. 1269-1276
Digital Object Identifier (DOI)doi:10.1016/j.febslet.2006.01.043
PubMed ID16455082
Open accessPublished as non-open access
Funder project or code502
ISSN00145793
PublisherWiley

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