| Autor: |
Sauer J; Institut für Mikrobiologie und Molekularbiologie der Justus-Liebig-Universität Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany., Schreiber U, Schmid R, Völker U, Forchhammer K |
| Jazyk: |
angličtina |
| Zdroj: |
Plant physiology [Plant Physiol] 2001 May; Vol. 126 (1), pp. 233-43. |
| DOI: |
10.1104/pp.126.1.233 |
| Abstrakt: |
Cells of the non-diazotrophic cyanobacterium Synechococcus sp. strain PCC 7942 acclimate to nitrogen deprivation by differentiating into non-pigmented resting cells, which are able to survive prolonged periods of starvation. In this study, the physiological properties of the long-term nitrogen-starved cells are investigated in an attempt to elucidate the mechanisms of maintenance of viability. Preservation of energetic homeostasis is based on a low level of residual photosynthesis; activities of photosystem II and photosystem I were approximately 0.1% of activities of vegetatively growing cells. The low levels of photosystem I activity were measured by a novel colorimetric assay developed from the activity staining of ferredoxin:NADP+ oxidoreductase. Photosystem II reaction centers, as determined by chlorophyll fluorescence measurements, exhibited normal properties, although the efficiency of light harvesting was significantly reduced compared with that of control cells. Long-term chlorotic cells carried out protein synthesis at a very low, but detectable level, as revealed by in vivo [35S]methionine labeling and two-dimensional gel electrophoresis. In conjunction with the very low levels of total cellular protein contents, this implies a continuous protein turnover during chlorosis. Synthesis of components of the photosynthetic apparatus could be detected, whereas factors of the translational machinery were stringently down-regulated. Beyond the massive loss of protein during acclimation to nitrogen deprivation, two proteins that were identified as SomA and SomB accumulated due to an induced expression following nitrogen reduction. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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