Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 8, pp 825–832

The ribonuclease A superfamily: general discussion

  • J. J. Beintema
  • R. G. Kleineidam

DOI: 10.1007/s000180050211

Cite this article as:
Beintema, J. & Kleineidam, R. CMLS, Cell. Mol. Life Sci. (1998) 54: 825. doi:10.1007/s000180050211

Abstract.

Enzymic properties of members of the ribonuclease A superfamily, like the activity on RNA, the preference for either cytosine or uracil in the primary binding site B1 , the preference for the other side of the cleaved phosphodiester bond, the B2 site, and features of the two noncatalytic phosphate-binding sites P0 and P2 are discussed in several articles in this multi-author review, and are summarized in this closing article. A special feature of members of the ribonucleases 1 family is their destabilizing action on double-stranded nucleic acid structures. A feature of the ribonuclease A superfamily is the frequent occurrence of gene duplications, both in ancestral vertebrate lineages and in recently evolved taxa. Three different bovine ribonucleases 1 have been identified in pancreas, semen and brain, respectively, which are the result of two gene duplications in an ancestral ruminant. Similar gene duplications have been identified in other ribonuclease families in several mammalian and other vertebrate taxa. The ribonuclease family, of which the human members have been assigned numbers 2, 3 and 6, underwent a still mysterious pattern of gene duplications and functional expression as proteins with ribonuclease activity and other physiological properties.

Key words. Ribonuclease A; pyrimidine base specificity; eosinophil-derived neurotoxin; eosinophil cationic protein; angiogenin; gene duplication. 

Copyright information

© Birkhäuser Verlag Basel, 1998

Authors and Affiliations

  • J. J. Beintema
    • 1
  • R. G. Kleineidam
    • 1
  1. 1.Biochemisch Laboratorium, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen (The Netherlands), Fax +31 50 3634165NL

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