Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1998-9-17
pubmed:abstractText
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 gamma and beta 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.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-1281549, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-165900, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-16789187, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-16789227, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-1779840, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-1848923, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-3739227, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-6138253, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-6254974, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-6389537, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-7754031, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-7769718, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8337833, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8352585, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8387208, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8444848, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8559059, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8662636, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8709242, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8718687, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8847498, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8898189, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-8987394, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9007052, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9038214, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9069265, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9139692, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9200605, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9275164, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9295359, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9299611, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9345280, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9371772, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9398072, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9407024, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9447962, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9473487, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9512541, http://linkedlifedata.com/resource/pubmed/commentcorrection/9707557-9545288
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acid Anhydride Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/CEL-1 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, http://linkedlifedata.com/resource/pubmed/chemical/RNA triphosphatase, http://linkedlifedata.com/resource/pubmed/chemical/RNA-tyrosine phosphatase, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/mRNA guanylyltransferase
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9808-12
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A protein tyrosine phosphatase-like protein from baculovirus has RNA 5'-triphosphatase and diphosphatase activities.
pubmed:affiliation
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't