Doublecortin, a brain-specific gene mutated in human x-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein

Article Abstract:

Research was conducted to investigate the synthesis of a de novo balanced translocation in a patient with X-linked lissencephaly and double cortex syndrome. Cosmids were selected for shotgun sequencing while polymerase chain reactions were performed on a nondenaturing acrylamide gel run. DNA sequencing was also performed in study using generalized techniques via an automated sequencer. Results of the study showed that the translocation characterized a novel predicted protein called Doublecortin.

author: Fox, Jeremy W., Walsh, Christopher A., Dobyns, William B., Gleeson, Joseph G., Allen, Kristina M., Lamperti, Edward D., Berkovic, Samuel, Scheffer, Ingrid, Cooper, Edward C., Minnerath, Sharon R., Ross, M. Elizabeth
Proteins, Brain diseases

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Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation

Article Abstract:

Purified mammalian and yeast Sec61p complexes in detergent form cylindrical oligomers with a diameter of approximately 85 angstroms and a central pore of approximately 20 angstroms. These cylindrical oligomers are proposed to represent protein-conducting channels of the endoplasmic reticulum membrane. Through electron microscopy, it was found that each oligomer contains 3-4 heterotrimers. The Sec61p complex's association with ribosomes or the Sec62/63p complex stimulates its oligomer formation.

author: Rapoport, Tom A., Plath, Kathrin, Jungnickel, Berit, Hanein, Dorit, Matlack, Kent E.S., Kalies, Kai-Uwe, Miller, Kenneth R., Akey, Christopher W.
Endoplasmic reticulum

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Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing

Article Abstract:

Research was conducted to determine the location and orientation of elongation factor G (EF-G) in the ribosome utilizing directed hydroxyl radical probing to understand the mechanism of EF-G-catalyzed translocation. Polymerase chain reaction was utilized to amplify the EF-G gene from the genomic DNA of Escherichia coli. Results showed that two of the rRNA targets were conserved parts of 23S rRNA that played a major role in elongation factor-dependent functions.

author: Noller, Harry F., Wilson, Kevin S.
Escherichia coli, Ribosomes, Hydroxylases

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subjects list: Research, Genetic aspects, Translocation (Genetics)
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