Effects of salicylic acid on protein content and 14C-amino acid incorporation into proteins of pea roots

Effects of salicylic acid on protein content and 14C-amino acid incorporation into proteins of... Pea (Pisum sativum L.) root treatment with salicylic acid (SA) changed the content of some proteins and incorporation of 14C-amino acids into proteins. The analysis of changes in these indices allowed us to subdivide all proteins into the four groups: (1) most abundant SA-independent proteins; (2) SA-dependent proteins, which content and 14C-amino acids incorporation both increased; (3) SA-dependent proteins, which content and 14C-amino acids incorporation both decreased; and (4) SA-dependent proteins, which content was not essentially changed (referred earlier to SA-independent proteins) but 14C-amino acids incorporation into these proteins was strongly suppressed. It is very likely that proteolysis of the proteins referred to the fourth group is very low and even a strong inhibition of their synthesis (incorporation of 14C-amino acids) does not result in the substantial decrease in their contents. Some SA-dependent proteins were identified by means of modern methods of proteomics: phosphoglyceromutase, S-adenosylmethionine synthase 3, enolase, chalcone isomerase, nucleoside diphosphate kinase 1, and tioredoxin h. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Effects of salicylic acid on protein content and 14C-amino acid incorporation into proteins of pea roots

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Publisher
Springer Journals
Copyright
Copyright © 2011 by Pleiades Publishing, Ltd.
Subject
Life Sciences; Plant Physiology; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1134/S1021443711040212
Publisher site
See Article on Publisher Site

Abstract

Pea (Pisum sativum L.) root treatment with salicylic acid (SA) changed the content of some proteins and incorporation of 14C-amino acids into proteins. The analysis of changes in these indices allowed us to subdivide all proteins into the four groups: (1) most abundant SA-independent proteins; (2) SA-dependent proteins, which content and 14C-amino acids incorporation both increased; (3) SA-dependent proteins, which content and 14C-amino acids incorporation both decreased; and (4) SA-dependent proteins, which content was not essentially changed (referred earlier to SA-independent proteins) but 14C-amino acids incorporation into these proteins was strongly suppressed. It is very likely that proteolysis of the proteins referred to the fourth group is very low and even a strong inhibition of their synthesis (incorporation of 14C-amino acids) does not result in the substantial decrease in their contents. Some SA-dependent proteins were identified by means of modern methods of proteomics: phosphoglyceromutase, S-adenosylmethionine synthase 3, enolase, chalcone isomerase, nucleoside diphosphate kinase 1, and tioredoxin h.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Jun 19, 2011

References

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