Histochemical Study of Enzyme Activity in the Shoot Apical Meristem of Brassica campestris L. During Transition to Flowering. II. Cytochrome Oxidase

1984 ◽  
Vol 145 (3) ◽  
pp. 308-311 ◽  
Author(s):  
Alan R. Orr
Planta ◽  
1980 ◽  
Vol 150 (5) ◽  
pp. 397-405 ◽  
Author(s):  
D. Pierard ◽  
A. Jacqmard ◽  
G. Bernier ◽  
J. Salmon

1968 ◽  
Vol 46 (2) ◽  
pp. 115-120 ◽  
Author(s):  
Abdul J. Mia ◽  
Suman M. Pathak

The Rauwolfia apical meristem has three zones which are cytologically recognizable, viz. tunica, corpus, and pith-cell meristem. Histochemically, however, these zonations are not discernible. The entire meristem either reacts positively or negatively for a particular enzyme. The apical meristem and procambial strands give a strong positive reaction for cytochrome oxidase, succinic dehydrogenase, and total protein. The pith cells react positively with peroxidase, acid phosphatase, and phosphorylase. Alkaline phosphatase is distributed throughout the meristematic and non-meristematic areas of the shoot apex. Cells in these areas appear to give slight reaction for glucose-6-phosphatase and 5-nucleotidase. Activities of several enzyme systems, such as cytochrome oxidase, peroxidase, succinic dehydrogenase, and acid phosphatase, were localized in the sclereid initials. Commonly the sclereids give more intensified enzymatic reaction than the pith parenchyma cells.


2018 ◽  
Author(s):  
Silvio Collani ◽  
Manuela Neumann ◽  
Levi Yant ◽  
Markus Schmid

ABSTRACTThe transition to flowering is a crucial step in the plant life cycle that is controlled by multiple endogenous and environmental cues, including hormones, sugars, temperature, and photoperiod. Permissive photoperiod induces FLOWERING LOCUS T (FT) in the phloem companion cells of leaves. The FT protein then acts as a florigen that is transported to the shoot apical meristem (SAM) where it physically interacts with the bZIP transcription factor FD and 14-3-3 proteins. However, despite the importance of FD for promoting flowering, its direct transcriptional targets are largely unknown. Here we combined ChIP-seq and RNA-seq to identify targets of FD at the genome-wide scale and assess the contribution of FT to binding DNA. We further investigated the ability of FD to form protein complexes with FT and TFL1 through the interaction with 14-3-3 proteins. Importantly, we observe direct binding of FD to targets involved in several aspects of the plant development not directly related to the regulation of flowering time. Our results confirm FD as central regulator of the floral transition at the shoot meristem and provides evidence for crosstalk between the regulation of flowering and other signaling pathways.Material DistributionThe author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.cell.com/molecular-plant/authors): Markus Schmid ([email protected]).Contact InformationUmeå Plant Science Centre (UPSC), Dept. of Plant Physiology Umeå University, SE-901 87 Umeå, SWEDEN


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