PMID- 19465686
OWN - NLM
STAT- MEDLINE
DCOM- 20090804
LR  - 20231127
IS  - 1469-9001 (Electronic)
IS  - 1355-8382 (Print)
IS  - 1355-8382 (Linking)
VI  - 15
IP  - 7
DP  - 2009 Jul
TI  - Novel TUTase associates with an editosome-like complex in mitochondria of 
      Trypanosoma brucei.
PG  - 1322-37
LID - 10.1261/rna.1538809 [doi]
AB  - Expression of mitochondrial genomes in Kinetoplastida protists requires massive 
      uracil insertion/deletion mRNA editing. The cascade of editing reactions is 
      accomplished by a multiprotein complex, the 20S editosome, and is directed by 
      trans-acting guide RNAs. Two distinct RNA terminal uridylyl transferases 
      (TUTases), RNA Editing TUTase 1 (RET1) and RNA Editing TUTase 2 (RET2), catalyze 
      3' uridylylation of guide RNAs and U-insertions into the mRNAs, respectively. 
      RET1 is also involved in mitochondrial mRNA turnover and participates in numerous 
      heterogeneous complexes; RET2 is an integral part of the 20S editosome, in which 
      it forms a U-insertion subcomplex with zinc finger protein MP81 and RNA editing 
      ligase REL2. Here we report the identification of a third mitochondrial TUTase 
      from Trypanosoma brucei. The mitochondrial editosome-like complex associated 
      TUTase (MEAT1) interacts with a 20S editosome-like particle, effectively 
      substituting the U-insertion subcomplex. MEAT1 and RET2 are mutually exclusive in 
      their respective complexes, which otherwise share several components. Similarly 
      to RET2, MEAT1 is exclusively U-specific in vitro and is active on gapped 
      double-stranded RNA resembling editing substrates. However, MEAT1 does not 
      require a 5' phosphate group on the 3' mRNA cleavage fragment produced by editing 
      endonucleases. The functional RNAi complementation experiments showed that MEAT1 
      is essential for viability of bloodstream and insect parasite forms. The growth 
      inhibition phenotype in the latter can be rescued by coexpressing an 
      RNAi-resistant gene with double-stranded RNA targeting the endogenous transcript. 
      However, preliminary RNA analysis revealed no gross effects on RNA editing in 
      MEAT1-depleted cells and indicated its possible role in regulating the 
      mitochondrial RNA stability.
FAU - Aphasizheva, Inna
AU  - Aphasizheva I
AD  - Department of Microbiology and Molecular Genetics, School of Medicine, University 
      of California at Irvine, Irvine, California 92697, USA.
FAU - Ringpis, Gene-Errol
AU  - Ringpis GE
FAU - Weng, James
AU  - Weng J
FAU - Gershon, Paul D
AU  - Gershon PD
FAU - Lathrop, Richard H
AU  - Lathrop RH
FAU - Aphasizhev, Ruslan
AU  - Aphasizhev R
LA  - eng
GR  - R01 AI064653/AI/NIAID NIH HHS/United States
GR  - AI064653/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20090522
PL  - United States
TA  - RNA
JT  - RNA (New York, N.Y.)
JID - 9509184
RN  - 0 (Protozoan Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Mitochondrial)
RN  - 0 (RNA, Protozoan)
RN  - 0 (RNA, Small Interfering)
RN  - 63231-63-0 (RNA)
RN  - EC 2.7.7.- (RNA Nucleotidyltransferases)
RN  - EC 2.7.7.- (UTP-RNA uridylyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Mitochondria/*enzymology
MH  - Molecular Sequence Data
MH  - Protozoan Proteins/*metabolism
MH  - RNA/genetics/metabolism
MH  - *RNA Editing
MH  - RNA Nucleotidyltransferases/antagonists & inhibitors/genetics/*metabolism
MH  - RNA, Messenger/genetics/*metabolism
MH  - RNA, Mitochondrial
MH  - RNA, Protozoan/*genetics
MH  - RNA, Small Interfering/pharmacology
MH  - Sequence Homology, Amino Acid
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Subcellular Fractions
MH  - Trypanosoma brucei brucei/*enzymology/genetics
PMC - PMC2704088
EDAT- 2009/05/26 09:00
MHDA- 2009/08/06 09:00
PMCR- 2010/01/01
CRDT- 2009/05/26 09:00
PHST- 2009/05/26 09:00 [entrez]
PHST- 2009/05/26 09:00 [pubmed]
PHST- 2009/08/06 09:00 [medline]
PHST- 2010/01/01 00:00 [pmc-release]
AID - rna.1538809 [pii]
AID - RA [pii]
AID - 10.1261/rna.1538809 [doi]
PST - ppublish
SO  - RNA. 2009 Jul;15(7):1322-37. doi: 10.1261/rna.1538809. Epub 2009 May 22.