Ontology type: schema:ScholarlyArticle
1987-05
AUTHORSJenq-Yunn Sheen, Lawrence Bogorad
ABSTRACTIn vitro translation of polyA(+) mRNAs isolated from purified maize bundle sheath and mesophyll cells results in the production of distinctive, cell-specific polypeptides. Immunoprecipitation experiments show that translatable polyA(+) mRNAs for phosphoenolpyruvate carboxylase (PEPC), pyruvate orthophosphate dikinase (PPDK) and NADP-malate dehydrogenase (MDH) are prominent in mesophyll but not bundle sheath cells. On the contrary, those for sedoheptulose-1,7-bisphosphatase (SBP), fructose-1,6-bisphosphatase (FBP), NADP-malic enzyme (ME) and the small subunit of ribulose-1,5-bisphosphate carboxylase (RuBPC SS) are present only in bundle sheath cells. Moreover, polyA(+) mRNAs encoding the 33 kD, 23 kD and 16 kD polypeptides of the oxygen-evolving complex (OE33, OE23 and OE16) and the light-harvesting chlorophyll a/b binding protein of photosystem II (LHCP II) are much more abundant in mesophyll than in bundle sheath cells. Northern blot analyses with cDNA clones of PEPC, PPDK, ME, RuBPC SS, OE33, OE23, OE16 and LHCP II are consistent with the conclusion that the cell-specific expression of these genes is regulated at the RNA level. The RNA level differences are especially dramatic in dark-grown maize seedlings after illumination for 24 h. More... »
PAGES227-238
http://scigraph.springernature.com/pub.10.1007/bf00015031
DOIhttp://dx.doi.org/10.1007/bf00015031
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