Rapid degradation of Pseudomonas fluorescens 1‐aminocyclopropane‐1‐carboxylic acid deaminase proteins expressed in transgenic Arabidopsis. Issue 2 (6th June 2014)
- Record Type:
- Journal Article
- Title:
- Rapid degradation of Pseudomonas fluorescens 1‐aminocyclopropane‐1‐carboxylic acid deaminase proteins expressed in transgenic Arabidopsis. Issue 2 (6th June 2014)
- Main Title:
- Rapid degradation of Pseudomonas fluorescens 1‐aminocyclopropane‐1‐carboxylic acid deaminase proteins expressed in transgenic Arabidopsis
- Authors:
- Kim, Kangmin
Park, Sung‐Hee
Chae, Jong‐Chan
Soh, Byoung Yul
Lee, Kui‐Jae - Abstract:
- <abstract abstract-type="main" id="fml12456-abs-0001"> <title>Abstract</title> <p>1‐Aminocyclopropane‐1‐carboxylate (ACC) deaminase is commonly produced by plant growth‐promoting rhizobacteria (PGPR) and has been suggested to facilitate the growth and stress tolerance of hosts via a reduction in levels of ethylene. However, the regulatory mechanism of ACC deaminase (AcdS) protein within host plant cells is largely unknown. Here, we demonstrated beneficial effects and post‐translational modification of PGPR‐originated AcdS proteins in plants. Compared with the wild‐type, transgenic <italic>Arabidopsis</italic> expressing the <italic>Pseudomonas fluorescens acdS</italic> (<italic>PfacdS</italic>) gene displayed increased root elongation and reduced sensitivity to 10 μM exogenous ACC, an ethylene precursor. <italic>Arabidopsis</italic> expressing <italic>PfacdS</italic> also showed increased tolerance to high salinity (150 mM NaCl). PfAcdS proteins accumulated in transgenic <italic>Arabidopsis</italic> were rapidly degraded, which was potentially mediated by the 26S proteasome pathway. The degradation of PfAcdS was alleviated in the presence of exogenous ACC. In conclusion, our data suggest that the plant growth‐promoting effects of bacterial AcdS proteins are potentially modulated via protein turnover inside the host plant cells. Such post‐translational modification plays a physiological role in the mutualistic interactions between microorganisms and plants in the rhizospheric<abstract abstract-type="main" id="fml12456-abs-0001"> <title>Abstract</title> <p>1‐Aminocyclopropane‐1‐carboxylate (ACC) deaminase is commonly produced by plant growth‐promoting rhizobacteria (PGPR) and has been suggested to facilitate the growth and stress tolerance of hosts via a reduction in levels of ethylene. However, the regulatory mechanism of ACC deaminase (AcdS) protein within host plant cells is largely unknown. Here, we demonstrated beneficial effects and post‐translational modification of PGPR‐originated AcdS proteins in plants. Compared with the wild‐type, transgenic <italic>Arabidopsis</italic> expressing the <italic>Pseudomonas fluorescens acdS</italic> (<italic>PfacdS</italic>) gene displayed increased root elongation and reduced sensitivity to 10 μM exogenous ACC, an ethylene precursor. <italic>Arabidopsis</italic> expressing <italic>PfacdS</italic> also showed increased tolerance to high salinity (150 mM NaCl). PfAcdS proteins accumulated in transgenic <italic>Arabidopsis</italic> were rapidly degraded, which was potentially mediated by the 26S proteasome pathway. The degradation of PfAcdS was alleviated in the presence of exogenous ACC. In conclusion, our data suggest that the plant growth‐promoting effects of bacterial AcdS proteins are potentially modulated via protein turnover inside the host plant cells. Such post‐translational modification plays a physiological role in the mutualistic interactions between microorganisms and plants in the rhizospheric and/or endospheric niche.</p> </abstract> … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 355:Issue 2(2014:Jun.)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 355:Issue 2(2014:Jun.)
- Issue Display:
- Volume 355, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 355
- Issue:
- 2
- Issue Sort Value:
- 2014-0355-0002-0000
- Page Start:
- 193
- Page End:
- 200
- Publication Date:
- 2014-06-06
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1111/1574-6968.12456 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3965.xml