PMID- 18191648
OWN - NLM
STAT- MEDLINE
DCOM- 20081014
LR  - 20231127
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1779
IP  - 4
DP  - 2008 Apr
TI  - Terminal RNA uridylyltransferases of trypanosomes.
PG  - 270-80
LID - 10.1016/j.bbagrm.2007.12.007 [doi]
AB  - Terminal RNA uridylyltransferases (TUTases) are functionally and structurally 
      diverse nucleotidyl transferases that catalyze template-independent 3' 
      uridylylation of RNAs. Within the DNA polymerase beta-type superfamily, TUTases 
      are closely related to non-canonical poly(A) polymerases. Studies of 
      U-insertion/deletion RNA editing in mitochondria of trypanosomatids identified 
      the first TUTase proteins and their cellular functions: post-transcriptional 
      uridylylation of guide RNAs by RNA editing TUTase 1 (RET1) and U-insertion mRNA 
      editing by RNA editing TUTase 2 (RET2). The editing TUTases possess conserved 
      catalytic and nucleotide base recognition domains, yet differ in quaternary 
      structure, substrate specificity and processivity. The cytosolic TUTases TUT3 and 
      TUT4 have also been identified in trypanosomes but their biological roles remain 
      to be established. Structural analyses have revealed a mechanism of cognate 
      nucleoside triphosphate selection by TUTases, which includes protein-UTP contacts 
      as well as contribution of the RNA substrate. This review focuses on biological 
      functions and structures of trypanosomal TUTases.
FAU - Aphasizhev, Ruslan
AU  - Aphasizhev R
AD  - Department of Microbiology and Molecular Genetics, School of Medicine, University 
      of California, Irvine, CA 92697-4025, USA. ruslan@uci.edu
FAU - Aphasizheva, Inna
AU  - Aphasizheva I
LA  - eng
GR  - R01 AI064653/AI/NIAID NIH HHS/United States
GR  - R01 AI064653-04/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 - 20071223
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Protozoan Proteins)
RN  - 0 (RNA, Mitochondrial)
RN  - 0 (RNA, Protozoan)
RN  - 27416-86-0 (Poly U)
RN  - 63231-63-0 (RNA)
RN  - EC 2.7.7.8 (Polyribonucleotide Nucleotidyltransferase)
RN  - UT0S826Z60 (Uridine Triphosphate)
SB  - IM
MH  - Animals
MH  - Mitochondria/genetics/metabolism
MH  - Mitochondrial Proteins/genetics/metabolism
MH  - Poly U/genetics/*metabolism
MH  - Polyribonucleotide Nucleotidyltransferase/genetics/*metabolism
MH  - Protein Structure, Tertiary/physiology
MH  - Protozoan Proteins/genetics/*metabolism
MH  - RNA/genetics/metabolism
MH  - RNA Editing/*physiology
MH  - RNA, Mitochondrial
MH  - RNA, Protozoan/genetics/*metabolism
MH  - Structure-Activity Relationship
MH  - Substrate Specificity/physiology
MH  - Trypanosoma/*enzymology/genetics
MH  - Uridine Triphosphate/genetics/metabolism
PMC - PMC2364610
MID - NIHMS47121
EDAT- 2008/01/15 09:00
MHDA- 2008/10/15 09:00
PMCR- 2009/04/01
CRDT- 2008/01/15 09:00
PHST- 2007/09/20 00:00 [received]
PHST- 2007/12/10 00:00 [revised]
PHST- 2007/12/13 00:00 [accepted]
PHST- 2008/01/15 09:00 [pubmed]
PHST- 2008/10/15 09:00 [medline]
PHST- 2008/01/15 09:00 [entrez]
PHST- 2009/04/01 00:00 [pmc-release]
AID - S1874-9399(07)00200-3 [pii]
AID - 10.1016/j.bbagrm.2007.12.007 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2008 Apr;1779(4):270-80. doi: 10.1016/j.bbagrm.2007.12.007. 
      Epub 2007 Dec 23.