By Giuseppe D’Alessio (auth.), Allen W. Nicholson (eds.)
Ribonucleases are a ubiquitous and functionally diversified 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 legislation, genome replication and upkeep, host safety, rigidity reaction, and viral ideas 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 via 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 yes disorder states. different issues comprise the evolutionary genetics and practical diversification of ribonucleases, engineered ribonucleases as anti-cancer brokers, the mechanisms of motion of man-made ribonucleases, and ribonucleases as types to appreciate protein folding and balance. This quantity should still function a necessary reference for a vast diversity of researchers and educators with pursuits in RNA metabolism, enzymology, and gene law.
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Additional resources for Ribonucleases
J Biol Chem 279(35):36753–36760 Simons BL, King MC, Cyr T, Hefford MA, Kaplan H (2002) Covalent cross-linking of proteins without chemical reagents. Protein Sci 11(6):1558–1564 Simons BL, Kaplan H, Fournier SM, Cyr T, Hefford MA (2007) A novel cross-linked RNase A dimer with enhanced enzymatic properties. Proteins 66(1):183–195 Sinatra F, Callari D, Viola M, Longombardo MT, Patania M, Litrico L, Emmanuele G, Lanteri E, D’Alessandro N, Travali S (2000) Bovine seminal RNase induces apoptosis in normal proliferating lymphocytes.
1), the other naturally antitumor RNase, is also resistant to RI (Wu et al. 1993) and (2) RNases with no cytotoxic activity, such as bovine RNase A or human RNase 1, with a very high affinity for RI, become cytotoxic when they are engineered into RI-resistant RNases (Antignani et al. 2001; Haigis et al. 2003; Leland et al. 1998; Piccoli et al. 1999; Suzuki et al. 1999). These results have led to the description of RI role in the cell as a sentry to guard cells from the entry in the cytosol of cytotoxic foreign RNases such as BS-RNase (Leland et al.
Obviously, the possibility cannot be excluded that in a gene sharing manner (Piatigorsky and Wistow 1991) ancestral RNases were involved both in angiogenesis and host defense. As for their 3D structures, determined by X-ray crystallography and model building, it has been found (Kazakou et al. 2008; Pizzo et al. 2010) that in some of them, the active site is partly obstructed as described for human angiogenin (see Sect. 4), a structural feature that is consistent with the low catalytic activity of human angiogenin, and zebrafish RNases as well.