Analysis of the non-sense mutants of varicella-zoster virus thymidine kinase

Analysis of the non-sense mutants of varicella-zoster virus thymidine kinase Three non-sense mutants of varicella-zoster virus (VZV) thymidine kinase (TK) gene, VZTK 325 , VZTK 278 and VZTK 224 , were isolated. The mutants had a single nucleotide substitution at codons 326, 279 and 225, which changed the codon of TGG (tryptophan) to the stop codon TGA. The wild type (WT) and mutant TKs were expressed in E. coli cells and their characteristics were evaluated. VZTK 224 lost TK activity, but VZTK 325 and VZTK 278 maintained 74.8% and 21.2% of the WT TK activity. On the other hand, all mutants lost the thymidylate kinase activity. Moreover, VZTK 325 and VZTK 278 polypeptides were heat-labile. These data suggest that the carboxy-terminal portion of herpesvirus TK plays an important role in the stable folding of TK and thymidylate kinase activity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Analysis of the non-sense mutants of varicella-zoster virus thymidine kinase

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Publisher
Springer-Verlag
Copyright
Copyright © Wien by 1997 Springer-Verlag/
Subject
Legacy
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s007050050223
Publisher site
See Article on Publisher Site

Abstract

Three non-sense mutants of varicella-zoster virus (VZV) thymidine kinase (TK) gene, VZTK 325 , VZTK 278 and VZTK 224 , were isolated. The mutants had a single nucleotide substitution at codons 326, 279 and 225, which changed the codon of TGG (tryptophan) to the stop codon TGA. The wild type (WT) and mutant TKs were expressed in E. coli cells and their characteristics were evaluated. VZTK 224 lost TK activity, but VZTK 325 and VZTK 278 maintained 74.8% and 21.2% of the WT TK activity. On the other hand, all mutants lost the thymidylate kinase activity. Moreover, VZTK 325 and VZTK 278 polypeptides were heat-labile. These data suggest that the carboxy-terminal portion of herpesvirus TK plays an important role in the stable folding of TK and thymidylate kinase activity.

Journal

Archives of VirologySpringer Journals

Published: Nov 1, 1997

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