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Biomed Res Int. 2013;2013:170398. doi: 10.1155/2013/170398. Epub 2013 Jan 17.

In silico prediction and in vitro characterization of multifunctional human RNase3.

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1
Institute of Molecular and Cellular Biology, National Tsing Hua University, No. 101, Section 2, Kuang Fu Road, Hsinchu 30013, Taiwan.

Abstract

Human ribonucleases A (hRNaseA) superfamily consists of thirteen members with high-structure similarities but exhibits divergent physiological functions other than RNase activity. Evolution of hRNaseA superfamily has gained novel functions which may be preserved in a unique region or domain to account for additional molecular interactions. hRNase3 has multiple functions including ribonucleolytic, heparan sulfate (HS) binding, cellular binding, endocytic, lipid destabilization, cytotoxic, and antimicrobial activities. In this study, three putative multifunctional regions, (34)RWRCK(38) (HBR1), (75)RSRFR(79) (HBR2), and (101)RPGRR(105) (HBR3), of hRNase3 have been identified employing in silico sequence analysis and validated employing in vitro activity assays. A heparin binding peptide containing HBR1 is characterized to act as a key element associated with HS binding, cellular binding, and lipid binding activities. In this study, we provide novel insights to identify functional regions of hRNase3 that may have implications for all hRNaseA superfamily members.

PMID:
23484086
PMCID:
PMC3581242
DOI:
10.1155/2013/170398
[Indexed for MEDLINE]
Free PMC Article
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