PMID- 10347225
OWN - NLM
STAT- MEDLINE
DCOM- 19990701
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 23
DP  - 1999 Jun 4
TI  - Human PIR1 of the protein-tyrosine phosphatase superfamily has RNA
      5'-triphosphatase and diphosphatase activities.
PG  - 16590-4
AB  - A human cDNA was isolated encoding a protein with significant sequence similarity
      (41% identity) to the BVP RNA 5'-phosphatase from the Autographa californica
      nuclear polyhedrosis virus. This protein is a member of the protein-tyrosine
      phosphatase (PTP) superfamily and is identical to PIR1, shown by Yuan et al.
      (Yuan, Y., Da-Ming, L., and Sun, H. (1998) J. Biol. Chem. 272, 20347-20353) to be
      a nuclear protein that can associate with RNA or ribonucleoprotein complexes. We 
      demonstrate that PIR1 removes two phosphates from the 5'-triphosphate end of RNA,
      but not from mononucleotide triphosphates. The specific activity of PIR1 with RNA
      is several orders of magnitude greater than that with the best protein substrates
      examined, suggesting that RNA is its physiological substrate. A 120-amino acid
      segment C-terminal to the PTP domain is not required for RNA phosphatase
      activity. We propose that PIR1 and its closest homologs, which include the
      metazoan mRNA capping enzymes, constitute a subgroup of the PTP family that use
      RNA as a substrate.
FAU - Deshpande, T
AU  - Deshpande T
AD  - Department of Biological Sciences, Purdue University, West Lafayette, Indiana
      47907, USA.
FAU - Takagi, T
AU  - Takagi T
FAU - Hao, L
AU  - Hao L
FAU - Buratowski, S
AU  - Buratowski S
FAU - Charbonneau, H
AU  - Charbonneau H
LA  - eng
SI  - GENBANK/AF023917
GR  - CA59935/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - EC 3.1.3.48 (DUSP11 protein, human)
RN  - EC 3.1.3.48 (Dual-Specificity Phosphatases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.6.- (Acid Anhydride Hydrolases)
RN  - EC 3.6.1.- (RNA triphosphatase)
SB  - IM
MH  - Acid Anhydride Hydrolases/*metabolism
MH  - Amino Acid Sequence
MH  - Catalytic Domain
MH  - Cell Line
MH  - Dual-Specificity Phosphatases
MH  - Escherichia coli
MH  - Glutathione Transferase/genetics/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Protein Tyrosine Phosphatases/genetics/*metabolism
MH  - Sequence Alignment
EDAT- 1999/05/29 00:00
MHDA- 1999/05/29 00:01
CRDT- 1999/05/29 00:00
PHST- 1999/05/29 00:00 [pubmed]
PHST- 1999/05/29 00:01 [medline]
PHST- 1999/05/29 00:00 [entrez]
AID - 10.1074/jbc.274.23.16590 [doi]
AID - S0021-9258(19)73010-5 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 4;274(23):16590-4. doi: 10.1074/jbc.274.23.16590.