Of proteins and RNA: The RNase P/MRP family

被引:170
作者
Esakova, Olga [1 ]
Krasilnikov, Andrey S. [1 ]
机构
[1] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
关键词
ribonuclease P; RNase P; ribonuclease MRP; RNase MRP; ribozyme; ribonucleoprotein; RIBONUCLEASE-P RNA; PRE-TRANSFER-RNA; CARTILAGE-HAIR HYPOPLASIA; PYROCOCCUS-HORIKOSHII OT3; PRECURSOR RIBOSOMAL-RNA; HUMAN LA ANTIGEN; MRP RIBONUCLEOPROTEIN COMPLEX; EXTERNAL GUIDE SEQUENCES; CELL-CYCLE PROGRESSION; METAL-BINDING SITE;
D O I
10.1261/rna.2214510
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
Nuclear ribonuclease (RNase) P is a ubiquitous essential ribonucleoprotein complex, one of only two known RNA-based enzymes found in all three domains of life. The RNA component is the catalytic moiety of RNases P across all phylogenetic domains; it contains a well-conserved core, whereas peripheral structural elements are diverse. RNA components of eukaryotic RNases P tend to be less complex than their bacterial counterparts, a simplification that is accompanied by a dramatic reduction of their catalytic ability in the absence of protein. The size and complexity of the protein moieties increase dramatically from bacterial to archaeal to eukaryotic enzymes, apparently reflecting the delegation of some structural functions from RNA to proteins and, perhaps, in response to the increased complexity of the cellular environment in the more evolutionarily advanced organisms; the reasons for the increased dependence on proteins are not clear. We review current information on RNase P and the closely related universal eukaryotic enzyme RNase MRP, focusing on their functions and structural organization.
引用
收藏
页码:1725 / 1747
页数:23
相关论文
共 273 条
[1]   RIBONUCLEASE-E PROVIDES SUBSTRATES FOR RIBONUCLEASE P-DEPENDENT PROCESSING OF A POLYCISTRONIC MESSENGER-RNA [J].
ALIFANO, P ;
RIVELLINI, F ;
PISCITELLI, C ;
ARRAIANO, CM ;
BRUNI, CB ;
CARLOMAGNO, MS .
GENES & DEVELOPMENT, 1994, 8 (24) :3021-3031
[2]   RNase P cleaves transient structures in some riboswitches [J].
Altman, S ;
Wesolowski, D ;
Guerrier-Takada, C ;
Li, Y .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (32) :11284-11289
[3]  
ALTMAN S, 1999, RNA WORLD, V2, P351
[4]   Solution Structure of Pyrococcus furiosus RPP21, a Component of the Archaeal RNase P Holoenzyme, and Interactions with Its RPP29 Protein Partner [J].
Amero, Carlos D. ;
Boomershine, William P. ;
Xu, Yiren ;
Foster, Mark .
BIOCHEMISTRY, 2008, 47 (45) :11704-11710
[5]   The two faces of Alba: the evolutionary connection between proteins participating in chromatin structure and RNA metabolism [J].
Aravind, L ;
Iyer, LM ;
Anantharaman, V .
GENOME BIOLOGY, 2003, 4 (10)
[6]   Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture [J].
Aspinall, Tanya V. ;
Gordon, James M. B. ;
Bennett, Hayley J. ;
Karahalios, Panagiotis ;
Bukowski, John-Paul ;
Walker, Scott C. ;
Engelke, David R. ;
Avis, Johanna M. .
NUCLEIC ACIDS RESEARCH, 2007, 35 (19) :6439-6450
[7]   Folding of a universal ribozyme: the ribonuclease P RNA [J].
Baird, Nathan J. ;
Fang, Xing-Wang ;
Srividya, Narayanan ;
Pan, Tao ;
Sosnick, Tobin R. .
QUARTERLY REVIEWS OF BIOPHYSICS, 2007, 40 (02) :113-161
[8]   Extended Structures in RNA Folding Intermediates Are Due to Nonnative Interactions Rather than Electrostatic Repulsion [J].
Baird, Nathan J. ;
Gong, Haipeng ;
Zaheer, Syed S. ;
Freed, Karl F. ;
Pan, Tao ;
Sosnick, Tobin R. .
JOURNAL OF MOLECULAR BIOLOGY, 2010, 397 (05) :1298-1306
[9]   Dimeric and monomeric Bacillus subtilis RNase P holoenzyme in the absence and presence of pre-tRNA substrates [J].
Barrera, A ;
Fang, XW ;
Jacob, J ;
Casey, E ;
Thiyagarajan, P ;
Pan, T .
BIOCHEMISTRY, 2002, 41 (43) :12986-12994
[10]   Magnesium ions are required by Bacillus subtilis ribonuclease P RNA for both binding and cleaving precursor tRNA(Asp) [J].
Beebe, JA ;
Kurz, JC ;
Fierke, CA .
BIOCHEMISTRY, 1996, 35 (32) :10493-10505