Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued

Cytoplasmic dynein is a microtubule-activated ATPase which produces force towards the minus ends of microtubules. It is thought to be responsible for retrograde axonal transport and other aspects of organelle motility and may have a role in the poleward movement of mitotic chromosomes. Cytoplasmic dynein is an oligomeric complex of two catalytic heavy chains and a number of accessory subunits. We now report the cloning and sequencing of a complementary DNA for one of these species, a cytoplasmic dynein-associated polypeptide of relative molecular mass 150,000 (Mr 150K). A full-length cDNA was found to contain an open reading frame of 4.0 kilobases, which is predicted to encode a polypeptide of Mr 145K. It has extensive homology with the product of the Drosophila gene Glued, which encodes a polypeptide of Mr 148K. The Glued mutation is dominant, with pleiotropic developmental defects in heterozygotes and an embryonic lethal phenotype in homozygotes. As dominant mutations may involve disruption of normal protein-protein interactions, the Glued mutation should provide insight into the mode of action of cytoplasmic dynein in vivo.     

Investigations of ZnO thin films deposited by a reactive pulsed laser ablation

Highly transparent ZnO thin films were deposited at different substrate temperatures by pulsed laser deposition in an oxygen atmosphere.The thin films were characterized by various techniques including X-ray diffraction,scanning electron microscopy,optical absorption,and photoluminescence.We demonstrated that oriented wurtzite ZnO thin films could be deposited at room temperature using a high purity zinc target.Variable temperature photoluminescence revealed new characteristics in the band edge emission.The...     

FDTD计算功率变换器近场到近/远场的转换

从理论上分析了利用时间有限差分法由近场到近场或远场转换的频域和时域两种方法，并选择时域的方法计算在FDTD计算范围内一给定点的电场值，与直接利用FDTD法得到的结果相比较，两者非常一致；最后利用该方法计算了功率变换器FDTD计算范围外一给定点的电磁场时间响应．     

Mutant dynactin in motor neuron disease

Impaired axonal transport in motor neurons has been proposed as a mechanism for neuronal degeneration in motor neuron disease. Here we show linkage of a lower motor neuron disease to a region of 4 Mb at chromosome 2p13. Mutation analysis of a gene in this interval that encodes the largest subunit of the axonal transport protein dynactin showed a single base-pair change resulting in an amino-acid substitution that is predicted to distort the folding of dynactin's microtubule-binding domain. Binding assays show decreased binding of the mutant protein to microtubules. Our results show that dysfunction of dynactin-mediated transport can lead to human motor neuron disease.