• Korean Journal of Breeding Science
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• v.50 no.4
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• pp.415-423
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• 2018

Rice panicle architecture is an important factor affecting yield potential. Korean rice cultivars have a narrow genetic background for panicle architecture. To enhance the yield potential of Korean rice cultivars, we developed and characterized rice lines with new panicle architecture. Rice with improved panicle architecture has clustered spikelets and dense panicles (CD type). CD rice was derived from a cross between "Binhae Col.#1" carrying dense panicles, and "ARC10319" that has the clustered spikelets gene (Cl). CD rice lines had short and semi-erect panicles with two to five high density spikelets clustered at the tips of primary and secondary rachis branches. CD rice lines had dramatically increased numbers of spikelets; almost twice as many as those of Korean rice cultivars. The increase in spikelet number was mainly caused by the increased spikelets and branches on secondary rachises compared to those on primary rachises. The increase in spikelet number was expected to enhance the yield of CD rice by expanding sink capacity. However, the yield of selected lines; CD9, CD27, CD34, and CD39, did not reach the level of the Korean high-yielding cultivars "Boramchan" and "Hanareum2," due to the reduction in panicle number and grain weight, and poor ripening. Although no substantial yield increase was observed in CD rice, the panicle architecture of CD rice, clustered spikelets, and dense panicles could be new genetic resources as breeding material for diversifying panicle architecture and enhancing yield potential.

• Journal of Life Science
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• v.32 no.2
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• pp.135-141
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• 2022

Thymosin β-4 (TB4) is a small peptide composed of 43 amino acids. To obtain sufficient biologically active mouse TB4 economically, we cloned and overexpressed this gene in an Escherichia coli system. With the isopropyl β-D-1-thiogalactopyranoside induction of the E. coli transformant, TB4 fusion protein with intein- and chitin-binding domain was successfully expressed in the soluble fraction within the E. coli cell. The TB4-intein - chitin-binding domain fusion protein was purified from the soluble fraction of E. coli cell lysate. The affinity chromatography with chitin beads and dithiothreitol-mediated intein self-cleavage reaction releases the TB4 peptide into the stripping solution. Sodium dodecyl sulphate - polyacrylamide gel electrophoresis and Western blot analyses were used to confirm that the recombinant TB4 peptide was produced with the expected size of 5 kDa. We found that the recombinant TB4 stimulated cell migration in the transwell plate chamber assay. After 18 hr of the treatment of the recombinant TB4 with 1 ng/ml concentration, the migration of the HT1080 cell was increased by 20% compared with that of the chemically synthesized TB4. The recombinant TB4 was also observed to promote the healing of a wound area in C57BL/6 mice by as high as 35% compared with that of the chemically synthesized TB4. These results suggest that the recombinant TB4 has better biological activity for cell migration and wound healing than that of the chemically synthesized TB4 peptide.