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 journalArticle

37 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

Fingerprint

Protein Tyrosine Phosphatases
Baculoviridae
RNA
Dual-Specificity Phosphatases
Proteins
mRNA guanylyltransferase
Phosphoric Monoester Hydrolases
Enzymes
Phosphates
Nucleopolyhedrovirus
Polynucleotides
Phosphoprotein Phosphatases
Mutant Proteins
Serine
Cysteine
Tyrosine
RNA triphosphatase
Catalytic Domain
Nucleotides

All Science Journal Classification (ASJC) codes

  • General

Cite this

A protein tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities. / Takagi, Toshimitsu; Taylor, Gregory S.; Kusakabe, Takahiro; Charbonneau, Harry; Buratowski, Stephen.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, No. 17, 18.08.1998, p. 9808-9812.

Research output: Contribution to journalArticle

@article{e9f87fc4e9f945e98399a0269a2a307f,
title = "A protein tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities",
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.",
author = "Toshimitsu Takagi and Taylor, {Gregory S.} and Takahiro Kusakabe and Harry Charbonneau and Stephen Buratowski",
year = "1998",
month = "8",
day = "18",
doi = "10.1073/pnas.95.17.9808",
language = "English",
volume = "95",
pages = "9808--9812",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "17",

}

TY - JOUR

T1 - A protein tyrosine phosphatase-like protein from baculovirus has RNA 5′-triphosphatase and diphosphatase activities

AU - Takagi, Toshimitsu

AU - Taylor, Gregory S.

AU - Kusakabe, Takahiro

AU - Charbonneau, Harry

AU - Buratowski, Stephen

PY - 1998/8/18

Y1 - 1998/8/18

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0032544081&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032544081&partnerID=8YFLogxK

U2 - 10.1073/pnas.95.17.9808

DO - 10.1073/pnas.95.17.9808

M3 - Article

C2 - 9707557

AN - SCOPUS:0032544081

VL - 95

SP - 9808

EP - 9812

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 17

ER -