PubMed · 13629102
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
1959-03-14. OCCUPATIONAL groups.. https://pubmed.ncbi.nlm.nih.gov/13629102/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Megagametogenesis of soybean, Glycine max (L.) Merr., cultivars Clark and Clark k2, and F1 hybrid of Clark (female parent) crossed with Clark k2 (male parent) were studied using stereo light microscopy and confocal scanning laser microscopy. Reproductive development in Clark and Clark k2 plants was compared to F1 hybrid plants. In mature pods, 6.4% of the ovules of Clark, 8.1% of the ovules of Clark k2, and 41.4% of the ovules of F1 hybrid plants were aborted. This female partial sterility was due to incomplete megagametophyte development: undeveloped polar nuclei-or developed but not in a position for fertilization; increased megagametophyte wall thickness; abnormal shape and/or premature degeneration of synergids and intact synergids throughout the life of the ovule; egg cell not well-developed or absent; and megagametophyte remaining uninucleate. Each of these abnormalities contributed to either lack of double fertilization or early megagametophyte abortion.
Recent discoveries show that LAT52 and LePRK2, two pollen-specific proteins, interact in what might be an autocrine signaling system. This exciting finding indicates that successful fertilization requires ligand-receptor kinase signals that regulate pollen-tube growth. The stage is now set to identify other components of this pathway and to explore their connections with the many signals exchanged between pollen and pistil.
The ubiquitin (Ub) system of intracellular protein degradation regulates the abundance of numerous proteins that control plant growth and development. Recent advances have begun to illustrate how environmental and endogenous signals affect plant responses through Ub-related proteolysis, the importance of combinatorial control in regulated protein destruction and how multiprotein complexes confer sensitivity and selectivity to ubiquitination. Further insight into the cell biology of Ub-chain assembly and proteasomal degradation, as well as into the relationship between proteolysis and other regulatory modifications, will be essential for understanding the mechanistic basis of the integration of diverse plant signals.