A protein tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities

Toshimitsu Takagi, Gregory S. Taylor, Takahiro Kusakabe, Harry Charbonneau, Stephen Buratowski

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

The superfamily of protein tyrosine phosphatases (PTPs) includes at least one enzyme with an RNA substrate. We recently showed that the RNA triphosphatase domain of the Caenorhabditis elegans mRNA capping enzyme is related to the PTP enzyme family by sequence similarity and mechanism. The PTP most similar in sequence to the capping enzyme triphosphatase is BVP, a dual-specificity PTP encoded by the Autographa californica nuclear polyhedrosis virus. Although BVP previously has been shown to have modest tyrosine and serine/threonine phosphatase activity, we find that it is much more potent as an RNA 5′-phosphatase. BVP sequentially removes γ and β phosphates from the 5′ end of triphosphate-terminated RNA, leaving a 5′-monophosphate end. The activity was specific for polynucleotides; nucleotide triphosphates were not hydrolyzed. A mutant protein in which the active site cysteine was replaced with serine was inactive. Three other dual-specificity PTPs (VH1, VHR, and Cdc14) did not exhibit detectable RNA phosphatase activity. Therefore, capping enzyme and BVP are members of a distinct PTP-like subfamily that can remove phosphates from RNA.

Original languageEnglish
Pages (from-to)9808-9812
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number17
DOIs
Publication statusPublished - Aug 18 1998

All Science Journal Classification (ASJC) codes

  • General

Fingerprint Dive into the research topics of 'A protein tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities'. Together they form a unique fingerprint.

Cite this