Abstract:
:Human eosinophil-derived neurotoxin (EDN) or RNase 2, found in the non-core matrix of eosinophils is a ribonuclease belonging to the Ribonuclease A superfamily. EDN manifests a number of bioactions including neurotoxic and antiviral activities, which are dependent on its ribonuclease activity. The core of the catalytic site of EDN contains various base and phosphate-binding subsites. Unlike many members of the RNase A superfamily, EDN contains an additional non-catalytic phosphate-binding subsite, P(-1). Although RNase A also contains a P(-1) subsite, the composition of the site in EDN and RNase A is different. In the current study we have generated site-specific mutants to study the role of P(-1) subsite residues Arg(36), Asn(39), and Gln(40) of EDN in its catalytic activity. The individual mutation of Arg(36), Asn (39), and Gln(40) resulted in a reduction in the catalytic activity of EDN on poly(U) and poly(C). However, there was no change in the activities on yeast tRNA and dinucleotide substrates. The study shows that the P(-1) subsite is crucial for the ribonucleolytic activity of EDN on polymeric RNA substrates.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Sikriwal D,Seth D,Dey P,Batra JKdoi
10.1007/s11010-007-9471-0subject
Has Abstractpub_date
2007-09-01 00:00:00pages
175-81issue
1-2eissn
0300-8177issn
1573-4919journal_volume
303pub_type
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