Ribulose-1,5-bisphosphate carboxylase/Oxygenase specific proteolysis in barley chloroplasts during dark induced senescence

Title:

Ribulose-1,5-bisphosphate carboxylase/Oxygenase specific proteolysis in barley chloroplasts during dark induced senescence

Creator:

Simova-Stoilova, L., Demirevska-Kepova, K., and Stoyanova, Z.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:c3869559-dc4b-4685-b471-04d7a68c34bc
uuid:c3869559-dc4b-4685-b471-04d7a68c34bc
issn:0300-3604
doi:10.1023/A:1024304103178

Subject:

ATP, biotinylated RuBPCO, dry/fresh mass ratio, EDTA, ELISA, Hordeum vulgare L., p-hydroxymercuribenzoate, Mg, phenyl-methyl sulphonyl fluoride, and proteolytic activity

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

Intact chloroplasts were isolated from dark-senescing primary barley (Hordeum vulgare L.) leaves in order to study selective ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCO) degradation by the stromal and membrane fractions. RuBPCO specific degradation was estimated and characterised applying sensitive avidin-biotin ELISA method with non-modified or oxidatively modified biotinylated RuBPCO (BR) as substrates. Distinct proteolytic activities were detected. They differed in ATP and divalent metal ion dependence, protease inhibitory profile, and dynamics in the time-course of dark-induced senescence. The results supported involvement of ATP- and metal ion-dependent serine type proteolytic activity against non-modified BR early in induced senescence and appearance of ATP-independent activity at later stage. Active oxygen-modified BR was degraded by ATP-independent serine-type protease probably containing essential SH-groups and requiring divalent metal ions. and L. Simova-Stoilova, K. Demirevska-Kepova, Z. Stoyanova.

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

561-566

Source:

Photosynthetica | 2002 Volume:40 | Number:4

Harvested from:

CDK

Metadata only:

false