RNA-specific ribonucleotidyl transferases

被引:171
作者
Martin, Georges [1 ]
Keller, Walter [1 ]
机构
[1] Univ Basel, Dept Cell Biol, Biozentrum, CH-4056 Basel, Switzerland
关键词
CCA-adding enzyme; poly(A) polymerase; RNA modification; terminal uridylyl transferase; 2'-5'-oligo(A) synthetase;
D O I
10.1261/rna.652807
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
RNA-specific nucleotidyl transferases (rNTrs) are a diverse family of template-independent polymerases that add ribonucleotides to the 3'-ends of RNA molecules. All rNTrs share a related active-site architecture first described for DNA polymerase beta and a catalytic mechanism conserved among DNA and RNA polymerases. The best known examples are the nuclear poly( A) polymerases involved in the 3'-end processing of eukaryotic messenger RNA precursors and the ubiquitous CCA- adding enzymes that complete the 3'- ends of tRNA molecules. In recent years, a growing number of new enzymes have been added to the list that now includes the "noncanonical'' poly(A) polymerases involved in RNA quality control or in the readenylation of dormant messenger RNAs in the cytoplasm. Other members of the group are terminal uridylyl transferases adding single or multiple UMP residues in RNA-editing reactions or upon the maturation of small RNAs and poly(U) polymerases, the substrates of which are still not known. 2'-5'Oligo(A) synthetases differ from the other rNTrs by synthesizing oligonucleotides with 2'-5'phosphodiester bonds de novo.
引用
收藏
页码:1834 / 1849
页数:16
相关论文
共 120 条
[21]  
DeLano W. L., 2002, PYMOL
[22]   Crystal structures of a template-independent DNA polymerase:: murine terminal deoxynucleotidyltransferase [J].
Delarue, M ;
Boulé, JB ;
Lescar, J ;
Expert-Bezançon, N ;
Jourdan, N ;
Sukumar, N ;
Rougeon, F ;
Papanicolaou, C .
EMBO JOURNAL, 2002, 21 (03) :427-439
[23]   Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei [J].
Deng, JP ;
Ernst, NL ;
Turley, S ;
Stuart, KD ;
Hol, WGJ .
EMBO JOURNAL, 2005, 24 (23) :4007-4017
[24]   Degradation of stable RNA in bacteria [J].
Deutscher, MP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (46) :45041-45044
[25]   A history of poly A sequences: From formation to factors to function [J].
Edmonds, M .
PROGRESS IN NUCLEIC ACID RESEARCH AND MOLECULAR BIOLOGY, VOL 71, 2002, 71 :285-389
[26]  
EDMONDS M, 1960, J BIOL CHEM, V235, P1142
[27]   U1 snRNP inhibits pre-mRNA polyadenylation through a direct interaction between U1 70K and poly(A) polymerase [J].
Gunderson, SI ;
Polycarpou-Schwarz, M ;
Mattaj, IW .
MOLECULAR CELL, 1998, 1 (02) :255-264
[28]   Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation [J].
Gunderson, SI ;
Vagner, S ;
PolycarpouSchwarz, M ;
Mattaj, IW .
GENES & DEVELOPMENT, 1997, 11 (06) :761-773
[29]   THE HUMAN U1A SNRNP PROTEIN REGULATES POLYADENYLATION VIA A DIRECT INTERACTION WITH POLY(A) POLYMERASE [J].
GUNDERSON, SI ;
BEYER, K ;
MARTIN, G ;
KELLER, W ;
BOELENS, WC ;
MATTAJ, IW .
CELL, 1994, 76 (03) :531-541
[30]   POLYADENYLYLATION DESTABILIZES THE RPSO MESSENGER-RNA OF ESCHERICHIA-COLI [J].
HAJNSDORF, E ;
BRAUN, F ;
HAUGELNIELSEN, J ;
REGNIER, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (09) :3973-3977