Nucleic Acids Research, Vol 24, Issue 18 3507-3513, Copyright © 1996 by Oxford University Press
HF Rosenberg and KD Dyer
The discovery of Ribonuclease k6 (RNase k6) was an unexpected result of our
ongoing efforts to trace the evolutionary history of the ribonuclease gene
family. The open reading frame of RNase k6, amplified from human genomic
DNA, encodes a 150 amino acid polypeptide with eight cysteines and
histidine and lysine residues corresponding to those found in the active
site of the prototype, ribonuclease A. The single- copy gene encoding RNase
k6 maps to human chromosome 14 and orthologous sequences were detected in
both primate and non-primate mammalian species. A single mRNA transcript
(1.5 kb) was detected in all human tissues tested, with lung representing
the most abundant source. At the cellular level, transcripts encoding RNase
k6 were detected in normal human monocytes and neutrophils (but not in
eosinophils) suggesting a role for this ribonuclease in host defense. Of
the five previously identified human ribonucleases of this group, RNase k6
is most closely related to eosinophil-derived neurotoxin (EDN), with 47%
amino acid sequence identity; slight cross-reactivity between RNase k6 and
EDN was observed on Western blots probed with polyclonal anti-EDN
antiserum. The catalytic constants determined, Km = 5.0 microM and Kcat =
0.13 s- 1, indicate that recombinant RNase k6 has approximately 40-fold
less ribonuclease activity than recombinant EDN. The identification and
characterization of RNase k6 has extended the ribonuclease gene family and
suggests the possibility that there are others awaiting discovery.
ARTICLES
Molecular cloning and characterization of a novel human ribonuclease (RNase k6): increasing diversity in the enlarging ribonuclease gene family
Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
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