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Plant Physiol, June 2000, Vol. 123, pp. 521-530
Immunolocalization of a Cysteine Protease in Vacuoles, Vesicles,
and Symbiosomes of Pea Nodule Cells1
Jason L.
Vincent and
Nicholas J.
Brewin*
Department of Genetics, John Innes Centre, Norwich Research Park,
Colney Lane, Norwich NR4 7UH, United Kingdom
PsCYP15A is a cysteine protease from pea (Pisum
sativum L.). It was first recognized as an up-regulated
transcript in wilted shoots and subsequently in root nodules containing
Rhizobium. Proteolytic activity of PsCYP15A in nodule
extracts is now reported following immunopurification with polyclonal
antiserum raised against recombinant antigen. Western-blot analysis
indicated two forms of PsCYP15A, a pro-form (approximately 38 kD) and a
mature form (approximately 30 kD). Both forms were present in most
tissue samples, but only the mature form was isolated from
cell-fractionated symbiosomes containing nitrogen-fixing bacteroids.
Immunolabeling of nodule sections showed localization of PsCYP15A
antigen in large vacuolar bodies, cytoplasmic vesicles, and the
perisymbiont space. Immunolabeling of tissue sections from wilted
shoots also indicated the presence of PsCYP15A in vacuoles and
cytoplasmic vesicles. This protease may be involved in the adaptation
to changes in cell turgor, both in wilted shoots and in nodule tissue.
Additionally, the protease may be involved in protein turnover in the
symbiosome compartment.
1
This work was supported by the UK Biotechnology
and Biological Research Council and by a Biotechnology and Biological
Science Research Council-funded post-graduate studentship (to J.L.V.).
*
Corresponding author; e-mail nick.brewin{at}bbsrc.ac.uk; fax
44-1603-450045.
© 2000 American Society of Plant Physiologists
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