Assembling the archaeal ribosome: roles for translation-factor-related GTPases

被引:15
作者
Blombach, Fabian [1 ]
Brouns, Stan J. J. [1 ]
van der Oost, John [1 ]
机构
[1] Wageningen Univ, Microbiol Lab, NL-6703 HB Wageningen, Netherlands
关键词
archaeon; GTPase; ribosome assembly; translation-factor-related GTPase (TRAFAC GTPase); GTP-BINDING PROTEIN; CIRCULARLY PERMUTED GTPASE; BACILLUS-SUBTILIS; CRYSTAL-STRUCTURE; ELONGATION-FACTOR; SUBUNIT; EVOLUTION; DOMAIN; OBG; REVEALS;
D O I
10.1042/BST0390045
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
The assembly of ribosomal subunits from their individual components (rRNA and ribosomal proteins) requires the assistance of a multitude of factors in order to control and increase the efficiency of the assembly process. GTPases of the TRAFAC (translation-factor-related) class constitute a major type of ribosome-assembly factor in Eukaryota and Bacteria. They are thought to aid the stepwise assembly of ribosomal subunits through a 'molecular switch' mechanism that involves conformational changes in response to GTP hydrolysis. Most conserved TRAFAC GTPases are involved in ribosome assembly or other translation-associated processes. They typically interact with ribosomal subunits, but in many cases, the exact role that these GTPases play remains unclear. Previous studies almost exclusively focused on the systems of Bacteria and Eukaryota. Archaea possess several conserved TRAFAC GTPases as well, with some GTPase families being present only in the archaeo-eukaryotic lineage. In the present paper, we review the occurrence of TRAFAC GTPases with translation-associated functions in Archaea.
引用
收藏
页码:45 / 50
页数:6
相关论文
共 46 条
[1]   Circularly permuted GTPase YqeH binds 30S ribosomal subunit: Implications for its role in ribosome assembly [J].
Anand, Baskaran ;
Surana, Parag ;
Bhogaraju, Sagar ;
Pahari, Sushmita ;
Prakash, Balaji .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2009, 386 (04) :602-606
[2]   Electrostatics of nanosystems: Application to microtubules and the ribosome [J].
Baker, NA ;
Sept, D ;
Joseph, S ;
Holst, MJ ;
McCammon, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (18) :10037-10041
[3]   The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].
Ban, N ;
Nissen, P ;
Hansen, J ;
Moore, PB ;
Steitz, TA .
SCIENCE, 2000, 289 (5481) :905-920
[4]   The NUG1 GTPase reveals an N-terminal RNA-binding domain that is essential for association with 60 S pre-ribosomal particles [J].
Bassler, Jochen ;
Kallas, Martina ;
Hurt, Ed .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (34) :24737-24744
[5]   THE GTPASE SUPERFAMILY - A CONSERVED SWITCH FOR DIVERSE CELL FUNCTIONS [J].
BOURNE, HR ;
SANDERS, DA ;
MCCORMICK, F .
NATURE, 1990, 348 (6297) :125-132
[6]   Role of GTPases in Bacterial Ribosome Assembly [J].
Britton, Robert A. .
ANNUAL REVIEW OF MICROBIOLOGY, 2009, 63 :155-176
[7]   Mesophilic crenarchaeota: proposal for a third archaeal phylum, the Thaumarchaeota [J].
Brochier-Armanet, Celine ;
Boussau, Bastien ;
Gribaldo, Simonetta ;
Forterre, Patrick .
NATURE REVIEWS MICROBIOLOGY, 2008, 6 (03) :245-252
[8]   Structural and biochemical analysis of the Obg GTP binding protein [J].
Buglino, J ;
Shen, V ;
Hakimian, P ;
Lima, CD .
STRUCTURE, 2002, 10 (11) :1581-1592
[9]   Function of the universally conserved bacterial GTPases [J].
Caldon, CE ;
March, PE .
CURRENT OPINION IN MICROBIOLOGY, 2003, 6 (02) :135-139
[10]   Stringent control in the archaeal genus Sulfolobus [J].
Cellini, A ;
Scoarughi, GL ;
Poggiali, P ;
Santino, I ;
Sessa, R ;
Donini, P ;
Cimmino, C .
RESEARCH IN MICROBIOLOGY, 2004, 155 (02) :98-104