Effects of photoinhibition and its recovery on photosynthetic functions of winter wheat (Triticum aestivum L.) under salt stress were studied. The results showed that several parameters associated with PSⅡ functions,...Effects of photoinhibition and its recovery on photosynthetic functions of winter wheat (Triticum aestivum L.) under salt stress were studied. The results showed that several parameters associated with PSⅡ functions, e.g. Fv/Fo?Fv/Fm and qP were not influenced by lower salt concentration (200 mmol/L NaCl) while CO 2 assimilation rate decreased significantly. When exposed to higher salt concentration (400 mmol/L NaCl), PSⅡ functions were significantly inhibited which led to the decrease of carbon assimilation. These results suggest that different concentrations of salt stress affected photosynthesis by different modes. Salt stress made photosynthesis more sensitive to strong light and led to more serious photoinhibition. Under lower concentration of salt stress, the Q B-non-reductive PSⅡ reaction centers formed at the beginning of photoinhibition could be effectively used to compose active PSⅡ reaction center (RC) and repair the reversible inactivated PSⅡ RC. Under higher concentration of salt stress, PSⅡ reaction centers were seriously damaged during photoinhibition, the Q B-non-reductive PSⅡ RC could only be partly effective at the early time of photoinhibition, thus led to the accumulation of Q B-non-reductive PSⅡ RC in the course of restoration under dim light.展开更多
RCAN1, also known as DSCR1, is an endogenous regulator of calcineurin, a serine/threonine protein phosphatase that plays a critical role in many physiological processes. In this report, we demonstrate that p38a MAP ki...RCAN1, also known as DSCR1, is an endogenous regulator of calcineurin, a serine/threonine protein phosphatase that plays a critical role in many physiological processes. In this report, we demonstrate that p38a MAP kinase can phosphorylate RCAN1 at multiple sites in vitro and show that phospho-RCAN1 is a good protein substrate for calcineurin. In addition, we found that unphosphorylated RCANI noncompetitively inhibits calcineurin protein phosphatase activity and that the phosphorylation of RCAN1 by p38a MAP kinase decreases the binding affinity of RCAN1 for calcineurin. These findings reveal the molecular mechanism by which p38a MAP kinase regulates the function of RCAN1/calcineurin through phosphorylation.展开更多
文摘Effects of photoinhibition and its recovery on photosynthetic functions of winter wheat (Triticum aestivum L.) under salt stress were studied. The results showed that several parameters associated with PSⅡ functions, e.g. Fv/Fo?Fv/Fm and qP were not influenced by lower salt concentration (200 mmol/L NaCl) while CO 2 assimilation rate decreased significantly. When exposed to higher salt concentration (400 mmol/L NaCl), PSⅡ functions were significantly inhibited which led to the decrease of carbon assimilation. These results suggest that different concentrations of salt stress affected photosynthesis by different modes. Salt stress made photosynthesis more sensitive to strong light and led to more serious photoinhibition. Under lower concentration of salt stress, the Q B-non-reductive PSⅡ reaction centers formed at the beginning of photoinhibition could be effectively used to compose active PSⅡ reaction center (RC) and repair the reversible inactivated PSⅡ RC. Under higher concentration of salt stress, PSⅡ reaction centers were seriously damaged during photoinhibition, the Q B-non-reductive PSⅡ RC could only be partly effective at the early time of photoinhibition, thus led to the accumulation of Q B-non-reductive PSⅡ RC in the course of restoration under dim light.
基金supported in part by Ministry of Science and Technology of China (Grant 2011CB910803)
文摘RCAN1, also known as DSCR1, is an endogenous regulator of calcineurin, a serine/threonine protein phosphatase that plays a critical role in many physiological processes. In this report, we demonstrate that p38a MAP kinase can phosphorylate RCAN1 at multiple sites in vitro and show that phospho-RCAN1 is a good protein substrate for calcineurin. In addition, we found that unphosphorylated RCANI noncompetitively inhibits calcineurin protein phosphatase activity and that the phosphorylation of RCAN1 by p38a MAP kinase decreases the binding affinity of RCAN1 for calcineurin. These findings reveal the molecular mechanism by which p38a MAP kinase regulates the function of RCAN1/calcineurin through phosphorylation.
