Nucleic Acids Research, Vol 25, Issue 21 4235-4239, Copyright © 1997 by Oxford University Press
D Batten, KD Dyer, JB Domachowske and HF Rosenberg
We have characterized four novel murine ribonuclease genes that, together
with the murine eosinophil-associated ribonucleases 1 and 2, form a
distinct and unusual cluster within the RNase A gene superfamily. Three of
these genes (mR-3, mR-4, mR-5) include complete open reading frames,
encoding ribonucleases with eight cysteines and appropriately spaced
histidines (His11 and His124) and lysine (Lys35) that are characteristic of
this enlarging protein family; the fourth sequence encodes a non-functional
pseudogene (mR-6P). Although the amino acid sequence similarities among
these murine ribonucleases varies from 60 to 94%, they form a unique
cluster, as each sequence is found to be more closely related to another of
this group than to either murine angiogenin or to murine pancreatic
ribonuclease. Interestingly, the relationship between the six genes in this
'mR cluster' and the defined lineages of the RNase A gene family could not
be determined by amino acid sequence homology, suggesting the possibility
that there are one or more additional ribonuclease lineages that have yet
to be defined. Although the nature of the evolutionary constraints
promoting this unusual expansion and diversification remain unclear, the
implications with respect to function are intriguing.
ARTICLES
Molecular cloning of four novel murine ribonuclease genes: unusual expansion within the ribonuclease A gene family
The Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
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