http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : Dongtao Liu (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
-
Xu, Tao,Sun, Xuewei,Jiang, Shiling,Ren, Dongtao,Liu, Guoqin Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.5
Kinesin is an ATP-driven microtubule motor protein that plays important roles in control of microtubule dynamics, intracellular transport, cell division and signal transduction. The kinesin superfamily is composed of numerous members that are classified into 14 subfamilies. Animal kinesins have been well characterized. In contrast, plant kinesins have not yet to be characterized adequately. Here, a novel plant-specific kinesin gene, GhKCH2, has been cloned from cotton (Gossypium hirsutum) fibers and biochemically identified by prokaryotic expression, affinity purification, ATPase activity assay and microtubule-binding analysis. The putative motor domain of GhKCH2, $M_{396-734}$ corresponding to amino acids Q396-N734 was fused with 6$\times$His-tag, soluble-expressed in E. coli and affinity-purified in a large amount. The biochemical analysis demonstrated that the basal ATPase activity of $M_{396-734}$ is not activated by $Ca^{2+}$, but stimulated 30-fold max by microtubules. The enzymatic activation is microtubule-concentration-dependent, and the concentration of microtubules that corresponds to half-maximum activation was about 11 ${\mu}M$, much higher than that of other kinesins reported. The cosedimentation assay indicated that $M_{396-734}$ could bind to microtubules in vitro whenever the nucleotide AMP-PNP is present or absent. As a plant-specific microtubule-dependent kinesin with a lower microtubule-affinity and a nucleotide-independent microtubule-binding ability, cotton GhKCH2 might be involved in the function of microtubules during the deposition of cellulose microfibrils in fibers or the formation of cell wall.
-
Jiang, Shiling,Li, Ming,Xu, Tao,Ren, Dongtao,Liu, Guoqin Korean Society for Biochemistry and Molecular Biol 2007 Journal of biochemistry and molecular biology Vol.40 No.1
Kinesins, as a kind of microtubule-based motor proteins, have a conserved microtubule-binding site in their motor domain. Here we report that two homologous kinesins in Arabidopsis thaliana, KatB and KatC, contain a second microtubule-binding site in their tail domains. The prokaryotic-expressed N-terminal tail domain of the KatC heavy chain can bind to microtubules in an ATP-insensitive manner. To identify the precise region responsible for the binding, a serious of truncated KatC cDNAs encoding KatC N-terminal regions in different lengths, KatC1-128, KatC1-86, KatC1-73 and KatC1-63, fused to Histidine-tags, were expressed in E. coli and affinity-purified. Microtubule cosedimentation assays show that the site at amino acid residues 74-86 in KatC is important for microtubule-binding. By similarity, we obtained three different lengths of KatB N-terminal regions, KatB1-384, KatB1-77, and KatB1-63, and analyzed their microtubule-binding ability. Cosedimentation assays indicate that the KatB tail domain can also bind to microtubules at the same site as and in a similar manner to KatC. Fluorescence microscopic observations show that the microtubule-binding site at the tail domain of KatB or KatC can induce microtubules bundling only when the stalk domain is present. Through pull-down assays, we show that KatB1-385 and KatC1-394 are able to interact specifically with themselves and with each other in vitro. These findings are significant for identifying a previously uncharacterized microtubule-binding site in the two kinesin proteins, KatB and KatC, and the functional relations between them.
-
Shuai Chen,Xiaohong Zhan,Yanqiu Zhao,Youfa Wu,Dongtao Liu 대한금속·재료학회 2021 METALS AND MATERIALS International Vol.27 No.6
Dual laser-beam bilateral synchronous welding is introduced to produce the 2.5 mm thick 5A90 Al–Li alloy T-joint. Thegrain morphology and grain size of weld metal (WM) in the T-joint are analyzed and calculated. The tensile experiment,scanning electron microscopy and energy disperse spectroscopy are respectively employed to study the tensile strength,fracture morphology and chemical composition of the T-joint. The results reveal that when the laser power is increased from2500 to 3000 W, the grain sizes of fine-grained layers and columnar dendrites near the fusion line are significantly reduced. Conversely, that of equiaxed dendrites at the WM center is not sensitive to the variety of laser power. Moreover, the degreeof elemental segregation in WM near the fusion line is also aggravated with the increasing of the laser power. The tensilestrength of the T-joint with the laser power of 2500 W is significantly higher than that with the laser power of 3000 W. Thetensile fracture locations are occurred in the weld toe with obvious pores, shear dimples and tear ridges, which are the typicalcharacteristics of ductile fracture. Besides, the chemical compositions of the second phase particles in the WM are moresensitive to than the variation of laser power compared with that of the matrix.
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
