How Zionism was Transformed in the U.S.
By Tim Heinz
Called "the most significant study of American Zionism to appear in a generation," Mark A. Raider�s recently published The Emergence of American Zionism (New York University Press) describes Zionism�s dramatic transformation in the American context.
Raider, assistant professor of modern and American Jewish history in the Department of Judaic Studies, is an expert on the relationship among American Jews, Zionism, and Israel. Through the use of much painstaking research conducted in the U.S. and Israel for this book, Raider traces how American Zionism changed from a marginal immigrant party at the turn of the 20th Century into a significant political force during World War II.
The book attempts to challenge many of the prevailing assumptions of Jewish and Zionist history that have remained popular for a full generation. It argues, for instance, that the Yishuv leadership and the Zionist pioneers in pre-state Israel, particularly the socialist Zionist movement known as "Labor Zionism," had a much more substantial impact on the American Jewish scene than had been previously recognized.
"I wanted to write a book that would be accessible to a popular audience and fill a big gap in Zionist and American Jewish history," said Raider, who joined the University faculty in Fall 1995.Jonathan D. Sarna, author of Religion and State in the American Jewish Experience, praised the work�s significance: "Overturning past wisdom, it demonstrates the centrality and vitality of Labor Zionism in American Jewish life, and also sheds fresh light on the culture and politics of Zionism in the American setting."
Raider addresses the ideas of how Zionism took shape in the U.S. and how Labor Zionism and the Yishuv influenced American Jews. His research depicts Labor Zionism�s dramatic transformation in the American context from a nonessential immigrant party into a significant political force.
The book also includes an unusual chapter about American Zionist propaganda, analyzing an array of publicity materials, posters, souvenirs, films, and fiction from the pre-state period.
According to Jehuda Reinharz, president of Brandeis University, the author has "deep insights about the relationship between the Yishuv leadership and American Jews. Raider persuasively makes the case that Zionism�s cultural vitality, intellectual diversity and unparalleled ability to rally public opinion in times of crisis were central to the American Jewish experience."
Mark Raider�s book The Emergence of American Zionism is now available at the Barnes & Noble University Bookstore.
Frank's 20-Year Search Produces Deepest Exploration of the Cell's Complex 'Factory'
For more than 40 years, scientists have studied the ribosome, the tiny "factory" within individual cells where proteins are made, but until recently no one had ever visualized it with any great clarity.
In the September-October issue of American Scientist magazine, cell biologist Joachim Frank of the Department of Biomedical Sciences in the School of Public Health tells how he and his colleagues produced a high-resolution reconstruction of one of nature�s most complex machines. His discoveries have, in turn, provided stunning insights into the life-sustaining process of protein synthesis.
Frank�s article, "How the Ribosome Works," describes his 20-year effort to develop the methods of cryo-electron microscopy (cryo-EM) and single-particle reconstruction that recently allowed him to see the ribosome in action. His data contributes to a growing body of evidence that RNA in the ribosome plays a more important role in protein synthesis than molecular biologists have traditionally appreciated.
A nationally honored Howard Hughes Medical Institute Investigator (biomedical science�s equivalent of a MacArthur Foundation "genius" award) and a researcher at the Wadsworth Center at the New York State Department of Health, Frank has research interests which range from electron optics and image-processing to three-dimensional reconstruction and ribosome structure and function.
A detailed description of how various components of the ribosome interact is important, because, as Frank observes, "Bacterial ribosomes are the targets of many antibiotics, and a better understanding of how the ribosome works will help towards making more efficient drugs." He said the imaging techniques employed by his lab are likely to prove useful in visualizing other complex cellular structures as well.
"Cryo-EM has given us the first three-dimensional map of the ribosome, and with it the first opportunity to integrate structural information with information obtained by a variety of biochemical and biophysical experiments," Frank wrote. "Moreover, cryo-EM allows us to visualize tRNA and protein factors attached to the ribosome in functionally meaningful complexes."
"With this information," he continued, "we can now test various models of how tRNA moves through the ribosome during protein synthesis. In essence, we have produced a series of snapshots of the ribosome as protein synthesis proceeds."
The three-dimensional computer images of a ribosome that illustrate the American Scientist article display a structure of bewildering complexity. Protein synthesis involves the proper interaction between DNA, RNA and numerous other molecules. The ribosome brings all of these components together in the proper spatial relation and ensures the orderly progression of protein synthesis. Visualizing this complex process is the key to understanding it.
Frank said that cryo-EM offers the advantage of preserving the ribosome molecule in its native state and revealing its interior features. The technique requires that the sample be maintained at extremely cold temperatures. A buffer solution containing ribosomes is dropped on a grid and frozen at the temperature of liquid nitrogen. The frozen grid is imaged in the electron microscope using a radiation dose so low that no damage is done to the sample. The resulting micrograph contains hundreds of ribosomes lying in different orientations.
Single-particle reconstruction involves manipulating the micrograph and computationally sorting all the varying views of ribosomes, which provides information about the molecule over its entire surface, and then integrating the resulting images to provide an initial low-resolution map of a ribosome.
The picture that has emerged of this basic mechanism of life indicates remarkable uniformity across species. "Barring an extraterrestrial origin of life, the ribosome and tRNA must have co-evolved during the first billion and a half years of life�s tenure on earth," Frank concluded.
"Neither the ribosome nor tRNA alone can accomplish translation, and the correct interaction between the two is absolutely vital for the survival of an organism � and by extension, a species. As life forms grew in complexity from the initial single-celled organisms to more sophisticated multi-cellular forms, their ribosomes also acquired some new bells and whistles in order to become more efficient. However, the tRNAs of plants and animals are virtually interchangeable with those in the bacterium E. coli."
In the last two years, Frank has also published landmark papers on the ribosome in Science and Nature magazines. He joined the Wadsworth Center laboratories as a research scientist in 1975 and the faculty of the School of Public Health a year later. He is currently chief of the Laboratory of Computational Biology and Molecular Imaging at Wadsworth.
American Scientist is an illustrated bimonthly magazine of science and technology published by Sigma Xi, the scientific research society.