By Giuseppe D’Alessio (auth.), Allen W. Nicholson (eds.)
Ribonucleases are a ubiquitous and functionally different crew of enzymes that experience a standard skill to cleave RNA. both via scission of inner phosphodiesters, or elimination of nucleotides from RNA five’ or three’ ends, ribonucleases practice crucial roles in gene expression and law, genome replication and upkeep, host safeguard, tension reaction, and viral innovations of an infection. Ribonucleases have additionally served as hugely informative versions to appreciate almost each element of biomolecular constitution and serve as. The fifteen chapters during this quantity are written by way of well-known researchers within the box, and supply in-depth analyses of the most important ribonuclease households. specific concentration is given to the relation of ribonuclease constitution and mechanism to organic functionality, in addition to ribonuclease disorder in convinced sickness states. different subject matters contain the evolutionary genetics and practical diversification of ribonucleases, engineered ribonucleases as anti-cancer brokers, the mechanisms of motion of synthetic ribonucleases, and ribonucleases as types to appreciate protein folding and balance. This quantity should still function an important reference for a extensive diversity of researchers and educators with pursuits in RNA metabolism, enzymology, and gene legislation.
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Extra info for Ribonucleases
Sample text
1998); then it moves to oocytes, where it is stored. An updated catalog of Rana family RNases has been recently proposed: It includes many members from Rana catesbeiana (Liao et al. 2000; Rosenberg et al. 2001), and a member from Rana pipiens, identified from a cDNA encoding an RNase expressed only in liver from female frogs (Chen et al. 2000). 1 Onconase Onconase (ONC, generic name ranpirnase) is a ribonuclease from the oocytes of Northern Leopard frogs (Rana pipiens) with cytotoxic activity toward tumor cells in vitro as well as in vivo in animal models; furthermore, it enhances sensitivity of tumor cells to several standard cytotoxic agents (Ardelt et al.
Protein Sci 9 (6):1217–1225 Vitagliano L, Merlino A, Zagari A, Mazzarella L (2002) Reversible substrate-induced domain motions in ribonuclease A. Proteins 46(1):97–104 Vottariello F, Costanzo C, Gotte G, Libonati M (2010) “Zero-length” dimers of ribonuclease A: further characterization and no evidence of cytotoxicity.
Acknowledgments I wish to thank my colleagues Tina Giancola, Guo-Fu Hu, Lelio Mazzarella, Antonello Merlino, Elio Pizzo, James F. Riordan, and Filomena Sica, who kindly contributed to improve the manuscript with their suggestions. References Abtin A, Eckhart L, Mildner M, Ghannadan M, Harder J, Schroder JM, Tschachler E (2009) Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7. J Investig Dermatol 129(9): 2193–2201 Acharya KR, Shapiro R, Allen SC, Riordan JF, Vallee BL (1994) Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease.