Sucrose Phosphate Synthase Expression at the Cell and Tissue Level Is Coordinated with Sucrose Sink-to-Source Transitions in Maize Leaf.
نویسندگان
چکیده
Immunohistological analyses for sucrose phosphate synthase (SPS) show that the protein is localized in both bundle-sheath cells (BS) and mesophyll cells (M) in maize (Zea mays) leaves. In young leaves, SPS protein was predominantly in the BS, whereas mature leaves showed nearly equal levels of signal in both BS and M. A cell-type-specific response was also seen in light and dark treatments. Dark treatments led to reduced signal in M; however, little or no change was detected in BS. We suggest that SPS in BS is engaged in sucrose biosynthesis by both photoassimilatory and starch turnover reactions in maize leaves. In addition, we suggest that the enzyme in BS may play a major role in the early biosynthesis of sucrose in young leaves. These cell-specific changes in expression in situ were in agreement with the estimates of extractable enzyme activity from isolated BS and M of mature leaves (R. Ohsugi, S.C. Huber [1987] Plant Physiol 84: 1096-1101). In contrast, western blot analyses did not show any significant changes in the levels of SPS protein in either young or mature leaves subsequent to similar dark treatments. It is interesting that the northern blot analyses indicate that the steady-state levels of SPS transcripts were markedly reduced after dark treatments of > 12 h. Overall, our results indicate that Sps gene expression in maize leaf is modulated at multiple levels of controls by both developmental and environmental factors.
منابع مشابه
Sucrose Synthase in Developing Maize Leaves: Regulation of Activity by Protein Level during the Import to Export Transition.
The maize (Zea mays) leaf is a valuable system to study the sucrose import to sucrose export transition at the cellular level. Rapidly growing and fully heterotrophic cells in the basal part of the young leaf showed a high sucrose synthase (SS) activity. Leaf SS has been purified to homogeneity. By comparison with purified kernel SS isozymes, the leaf SS has been identified as SS(2). SS(1) prot...
متن کاملBiosynthesis of Sucrose and Mannitol as a Function of Leaf Age in Celery (Apium graveolens L.).
In celery (Apium graveolens L.), the two major translocated carbohydrates are sucrose and the acyclic polyol mannitol. Their metabolism, however, is different and their specific functions are uncertain. To compare their roles in carbon partitioning and sink-source transitions, developmental changes in (14)CO(2) labeling, pool sizes, and key enzyme activities in leaf tissues were examined. The p...
متن کاملElevated sucrose-phosphate synthase activity in
Constitutive over-expression of a maize sucrosephosphate synthase (SPS) gene in tobacco (Nicotiana tabacum) had major effects on leaf carbohydrate budgets with consequences for whole plant development. Transgenic tobacco plants ̄owered earlier and had greater ̄ower numbers than wild-type plants. These changes were not linked to modi®ed source leaf carbon assimilation or carbon export, although ...
متن کاملElevated sucrose-phosphate synthase activity in transgenic tobacco sustains photosynthesis in older leaves and alters development.
Constitutive over-expression of a maize sucrose-phosphate synthase (SPS) gene in tobacco (Nicotiana tabacum) had major effects on leaf carbohydrate budgets with consequences for whole plant development. Transgenic tobacco plants flowered earlier and had greater flower numbers than wild-type plants. These changes were not linked to modified source leaf carbon assimilation or carbon export, altho...
متن کاملSer162-Dependent inactivation of overproduced sucrose-phosphate synthase protein of maize leaf in transgenic rice plants.
To investigate the role of Ser162 in phosphorylation-dependent regulation of maize sucrose-phosphate synthase (SPS) activities in rice, transgenic rice plants expressing wild-type or mutagenized maize SPS were produced. Our results indicate that Ser162 was responsible for overproduction-induced inactivation of SPS protein and for light/ dark modulation of this protein in vivo.
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Plant physiology
دوره 111 4 شماره
صفحات -
تاریخ انتشار 1996