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J. Biol. Chem., Vol. 266, Issue 23, 15293-15299, 08, 1991
SK Ghosh, J Kusari, SK Bandyopadhyay, H Samanta, R Kumar and GC Sen
2'-5'-oligoadenylate synthetases constitute a multimember family of
interferon-inducible enzymes which need double-stranded RNA as an
obligatory cofactor. We have isolated cDNA clones for two new murine
synthetases. These two clones, 9-2 and 3-9, encoded proteins of 414 and 363
amino acid residues, respectively, out of which the amino terminal 346
residues were almost identical. They were also very similar to the
corresponding regions of human synthetases E16 and E18. On the other hand,
the carboxyl-terminal 68 residues of clone 9-2 had no homology with the
carboxyl-terminal residues of E18. These murine clones had only 67% amino
acid identity with the previously isolated murine synthetase clone L3. 9-2
and 3-9 proteins were expressed efficiently by in vitro transcription and
translation of cDNA clones containing the synthetase coding regions
preceded by the 5'-untranslated region of the vesicular stomatitis virus NS
gene. These in vitro synthetized proteins bound to double-stranded RNA and
catalyzed the synthesis of 2'-5' oligoadenylates. A nested set of deletion
mutants of the 9-2 clone was produced by restriction digestion and
polymerase chain reaction. Functional testing of the corresponding
truncated proteins revealed that a region between amino acid residues 104
and 158 was necessary for binding to double-stranded RNA and a region
between residues 320 and 344 was necessary for enzyme activity. Moreover
substitution of the lysine residue at position 333 by arginine did not
affect the enzyme activity.
Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships
Department of Molecular Biology, Cleveland Clinic Foundation, Ohio 44195.
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