EFFECT OF AEROBIC PRIMING ON THE RESPONSE OF ECHINOCHLOA-CRUS-PAVONISTO ANAEROBIC STRESS - PROTEIN-SYNTHESIS AND PHOSPHORYLATION

Citation
F. Zhang et al., EFFECT OF AEROBIC PRIMING ON THE RESPONSE OF ECHINOCHLOA-CRUS-PAVONISTO ANAEROBIC STRESS - PROTEIN-SYNTHESIS AND PHOSPHORYLATION, Plant physiology, 105(4), 1994, pp. 1149-1157
Citations number
41
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
00320889
Volume
105
Issue
4
Year of publication
1994
Pages
1149 - 1157
Database
ISI
SICI code
0032-0889(1994)105:4<1149:EOAPOT>2.0.ZU;2-W
Abstract
Echinochloa species differ in their ability to germinate and grow in t he absence of oxygen. Seeds of Echinochloa crus-pavonis (H.B.K.) Schul t do not germinate under anoxia but remain viable for extended periods (at least 30 d) when incubated in an anaerobic environment. E. crus-p avonis can be induced to germinate and grow in an anaerobic environmen t if the seeds are first subjected to a short (1-18 h) exposure to aer obic conditions (aerobic priming). Changes in polypeptide patterns (co nstitutive and de novo synthesized) and protein phosphorylation induce d by aerobic priming were investigated. In the absence of aerobic prim ing protein degradation was not evident under anaerobic conditions, al though synthesis of a 20-kD polypeptide was induced. During aerobic pr iming, however, synthesis of 37- and 55-kD polypeptides was induced an d persisted upon return of the seeds to anoxia. Furthermore, phosphory lation of two 18-kD polypeptides was observed only in those seeds that were labeled with (PO4)-P-32 during the aerobic priming period. Subse quent chasing in an anaerobic environment resulted in a decrease in ph osphorylation of these polypeptides. Likewise, phosphorylation of the 18-kD polypeptides was not observed if the seeds were labeled in an an aerobic atmosphere. These results suggest that the regulated induction of the 20-, 37-, and 55-kD polypeptides may be important for anaerobi c germination and growth of E. crus-pavonis and that the specific phos phorylation of the 18-kD polypeptides may be a factor in regulating th is induction.