• KOREAN JOURNAL OF CROP SCIENCE
• /
• v.43 no.2
• /
• pp.59-63
• /
• 1998

Three different male-sterile cytoplasmic lines and their common maintainer 'Zhenshan 97B' and two elite restorer lines were used to study cytoplasmic effects on agronomic trait manifestation per se under different nitrogen supply levels. The result showed that cytoplasmic effects could be modified by nitrogen environments. The cytoplasmic effect on grain yield under 150 kg N/ha varied depending on crosses, while it was significantly negative in most crosses under both 60 and 330 kg N/ha. The correlation and path-coefficient analyses suggested that it was expected to improve cytoplasmic effects through reducing maximum tillers and increasing the percentage of productive tillers, leading to increased productive tillers and higher yield in hybrid rice by the aid of cultural practice and genetic transformation. This study also revealed that the same cytoplasm in different combinations had differential effect under the same nitrogen environment, indicating that cytoplasmic effect was produced by interaction of nuclear genes with cytoplasm rather than cytoplasm per se. These results indicated the usefulness of evaluating diverse cytoplasmic sources in various nuclear genotypes bred for hybrid rice breeding program. The finding also suggested that negative cytoplasmic effect could be effectively overcome by elite restorer lines through the interaction of nuclear genes with female cytoplasm.

• Molecules and Cells
• /
• v.43 no.11
• /
• pp.899-908
• /
• 2020

Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research.

• Molecules and Cells
• /
• v.26 no.3
• /
• pp.291-298
• /
• 2008

Human karyopherin ${\beta}3$, highly homologous to a yeast protein secretion enhancer (PSE1), has often been reported to be associated with a mediator of a nucleocytoplasmic transport pathway. Previously, we showed that karyopherin ${\beta}3$ complemented the PSE1 and KAP123 double mutant. Our research suggested that karyopherin beta has an evolutionary function similar to that of yeast PSE1 and/or KAP 123. In this study, we performed yeast two-hybrid screening to find a protein which would interact with karyopherin ${\beta}3$ and identified apolipoprotein A-I (apo A-I), a secretion protein with a primary function in cholesterol transport. By using in vitro binding assay, co-immunoprecipitation, and colocalization studies, we defined an interaction between karyopherin ${\beta}3$ and apo A-I. In addition, overexpression of karyopherin ${\beta}3$ significantly increased apo A-I secretion. These results suggest that karyopherin ${\beta}3$ plays a crucial role in apo A-I secretion. These findings may be relevant to the study of a novel function of karyopherin ${\beta}3$ and coronary artery diseases associated with apo A-I.

• Journal of the Korea Academia-Industrial cooperation Society
• /
• v.9 no.6
• /
• pp.1795-1799
• /
• 2008

The heterogeneous nuclear ribonucleoprotein K (hnRNP K) is a component of hnRNP complexes. This protein binds strongly to cytidine-rich RNA/DNA sequences. It is a nucleocytoplasmic shuttling protein. To investigate the functions of hnRNP K, I searched for hnRNP K-interacting proteins in HeLa cDNA library using a yeast two-hybrid screening system. One of the cDNA clones is identical to human hnRNP E1 (poly(rC) binding protein 1) cDNA (GenBank accession number XM_031585). In this study, hnRNP K is shown to specifically interact with hnRNP E1 in yeast two-hybrid system and in vitro biochemical assay.