Ribonucleases : Structures and junctions , edited by Giuseppe D ' Alessio and

Abstract

Our understanding of ribonucleases is simultaneously more advanced and more primitive than is our knowledge of RNA polymerases. Advanced. because ribonuclease A (RNase A) was one of the first enzymes to be discovered (in 1920), isolated (1938), and crystallized (1939), and has contributed many paradigms to protein science and enzymology. Primitive, because ribonucleases have important and, until recently, unappreciated roles in post-transcriptional control as well as in other biological processes. With this dichotomy of understanding, now is the perfect time to devote a volume solely to ribonucleases. Giuseppe D' Alessio and James F. Riordan have done just that, editing a book of 19 chapters . entitled: Ribonucleases: Structures and Functions. The book begins with a discussion of the gallery of Escherichia coli ribonucleases. These enzymes provide the best opportunity for understanding how ribonuc1eases regulate RNA levels by the degradation of RNA. The prevailing question is: how do ribonucleases distinguish between mRNAs destined to have half-lives that range from seconds to days? Exciting progress is being made in answering this question in bacteria (Chapter 1), as well as in yeast (Chapter 18). plants (Chapter 5), and mammals (Chapters 16 and 17). It is noteworthy that Chapter 16 is the first comprehensive review of the fascinating enzyme RNase L, which relies on RNA effectors with 2' -; 5' intemucleotide linkages. Several of the ribonucleases secreted by microbes have been studied in detail. Lacking the complexities imposed by disulfide bonds and cis prolyl peptide bonds, bamase has yielded much important infonnation about rudimentary aspects of protein folding. These data and the tight interaction of barnase with its natural inhibitor protein, barstar, provide the gist of Chapter 2. Barnase belongs to the RNase T I superfamily of enzymes. Recent advances in the enzymology of this superfamily are presented in Chapter 3. The structures and functions of a-sarcin and the related Aspergillus toxins restrictocin and mitogillin are recapped lucidly in Chapter 4. RNase A has been the most studied enzyme of the 20th century. These studies have generated many paradigms in biochemistry and biophysics. The voluminous amount of infonnation available on

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@inproceedings{Raines2001RibonucleasesS, title={Ribonucleases : Structures and junctions , edited by Giuseppe D ' Alessio and}, author={Tracy Raines}, year={2001} }