Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 471, Issue 2, Pages 191-197Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.12.016
Keywords
human pancreatic ribonuclease; substrate cleavage preference; non-catalytic binding subsites; site-directed mutagenesis
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Analyzing the pattern of oligonucleotide formation induced by HP-RNase cleavage shows that the enzyme does not act randomly and follows a more endonucleolytic pattern when compared to RNase A. The enzyme prefers the binding and cleavage of longer substrate molecules, especially when the phosphodiester bond that is broken is 8-11 nucleotides away from at least one of the ends of the substrate molecule. This more endonucleolytic pattern is more appropriate for an enzyme with a regulatory role. Deleting two positive charges oil the N-terminus (Arg4 and Lys6) modifies this pattern of external/internal phosphodiester bond cleavage preference, and produces a more exonucleolytic enzyme. These residues may reinforce the strength of a non-catalytic secondary phosphate binding (p(2)) or, alternatively, constitute a new non-catalytic phosphate binding subsite (p(3)). (C) 2007 Elsevier Inc. All rights reserved.
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