Human pancreatic ribonuclease presents higher endonucleolytic activity than ribonuclease A

M. Rodríguez, M. Moussaoui, A. Benito, C. M. Cuchillo, M. V. Nogués, M. Vilanova

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

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 on 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 (p2) or, alternatively, constitute a new non-catalytic phosphate binding subsite (p3). © 2007 Elsevier Inc. All rights reserved.
Original languageEnglish
Pages (from-to)191-197
JournalArchives of Biochemistry and Biophysics
Volume471
DOIs
Publication statusPublished - 15 Mar 2008

Keywords

  • Human pancreatic ribonuclease
  • Non-catalytic binding subsites
  • Site-directed mutagenesis
  • Substrate cleavage preference

Fingerprint Dive into the research topics of 'Human pancreatic ribonuclease presents higher endonucleolytic activity than ribonuclease A'. Together they form a unique fingerprint.

Cite this