Send to

Choose Destination
Planta. 1982 Sep;154(5):435-40. doi: 10.1007/BF01267810.

Protein turnover in the attached leaves of non-stressed and stressed barley seedlings.

Author information

School of Biological Sciences, University of East Anglia, NR4 7TJ, Norwich, UK.


Protein turnover was examined, using tritiated water, in various 2-cm regions of 7-11-d-old, first leaves of barley (Hordeum vulgare). Differences were found between the regions in their protein turnover and their responses to stress. The rate constant for degradation for total protein was the same throughout the leaf and the average half-life (t1/2) of protein=approx. 220 h. Only in the older regions did a 24-h pulse of(3)H2O preferentially label protein with a t1/2 (90 h) considerably shorter than the t1/2 for total protein. 'Soluble' protein was degraded faster than 'insoluble' protein and contained an appreciable short-lived protein component observable by short-pulse labelling. The rate of protein synthesis was greatest in the cells of the youngest region and declined as each region aged. The mean rate of protein synthesis over the 4-d period was 4 and 7 nmol h(-1) of amino-N with respect to the regions 1-3 and 7-9 cm from the leaf tip. Seedlings, stressed by adding polyethylene glycol (2.0 MPa) to the roots, showed a marked loss of protein from the older leaf regions with only small losses in the younger regions. Amino acids accumulated in the younger region continuously whereas in the older region little accumulation occurred until day 3 of stress when proline levels increased. Protein synthesis was decreased by between 30% and 50% in all leaf regions. In the region 1-3 cm from the leaf tip, the rate of protein degradation of total protein was enhanced and equalled the rate of degradation of 24-h-pulse-labelled protein which was not itself significantly affected by stress (t1/2=approx. 90 h). In the region 3-5 cm, the degradation of both 4-d and 24-h-labelled protein was enhanced by stress to rates similar to those found in the region 1-3 cm. This was largely through increases in the degradation of the 'insoluble' protein, but the degradation of 'soluble' protein was also raised. Protein degradation in the region 7-9 cm was not affected by stress.


Supplemental Content

Loading ...
Support Center