Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2016909 | Plant Science | 2016 | 28 Pages |
Abstract
Caseinolytic proteases (Clps) perform the important role of removing protein aggregates from cells, which can otherwise prove to be highly toxic. ClpD system is a two-component protease complex composed of a regulatory ATPase module ClpD and a proteolytic component ClpP. Under desiccation stress condition, rice ClpD1 (OsClpD1) gene encoding for the regulatory subunit, was represented by four variant transcripts differing mainly in the expanse of their N-terminal amino acids. These transcripts were expressed in a differential manner in response to salt, mannitol and polyethylene glycol stresses in rice. Purified OsClpD1.3 protein exhibited intrinsic chaperone activity, shown using citrate synthase as substrate. Arabidopsis (Col-0) plants over-expressing OsClpD1.3 open reading frame downstream to CaMV35S promoter (ClpD1.3 plants) showed higher tolerance to salt and desiccation stresses as compared to wild type plants. ClpD1.3 seedlings also showed enhanced growth during the early stages of seed germination under unstressed, control conditions. The free proline levels and starch breakdown activities were higher in the ClpD1.3 seedlings as compared to the wild type Arabidopsis seedlings. It thus emerges that increasing the potential of ClpD1 chaperoning activity may be of advantage in protection against abiotic stresses.
Keywords
Oryza sativaneomycin phosphotransferase IIisopropylthio-β-galactosidepyrroline-5-carboxylate synthasesqRT-PCRnptIIPB1NBDChaperoneP5CSCLPGSTProDHIPTGDASORFArabidopsis thalianaAlpha amylaseOsmotic stressAMYSalt stressnucleotide binding domainDAGdays after germinationCitrate synthaseopen reading frameReactionCaseinolytic proteaseproline dehydrogenasePoly ethylene glycolPEGglutathione S-transferase
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Ratnesh Chandra Mishra, Richa Richa, Anil Grover,