Reconstitution reveals the functional core of mammalian eIF3

被引:162
作者
Masutani, Mamiko
Sonenberg, Nahum
Yokoyama, Shigeyuki
Imataka, Hiroaki
机构
[1] RIKEN, Genom Sci Ctr, Prot Res Grp, Tsurumi Ku, Kanagawa 2300045, Japan
[2] McGill Univ, Dept Biochem, Montreal, PQ, Canada
[3] McGill Univ, McGill Canc Ctr, Montreal, PQ, Canada
[4] Univ Tokyo, Dept Biophys & Biochem, Bunkyo Ku, Tokyo, Japan
关键词
eIF; eIF3; reconstitution; translation; initiation;
D O I
10.1038/sj.emboj.7601765
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
Eukaryotic translation initiation factor (eIF) 3 is the largest eIF (similar to 650 kDa), consisting of 10-13 different polypeptide subunits in mammalian cells. To understand the role of each subunit, we successfully reconstituted a human eIF3 complex consisting of 11 subunits that promoted the recruitment of the 40S ribosomal subunit to mRNA. Strikingly, the eIF3g and eIF3i subunits, which are evolutionarily conserved between human and the yeast Saccharomyces cerevisiae are dispensable for active mammalian eIF3 complex formation. Extensive deletion analyses suggest that three evolutionarily conserved subunits (eIF3a, eIF3b, and eIF3c) and three non-conserved subunits (eIF3e, eIF3f, and eIF3h) comprise the functional core of mammalian eIF3.
引用
收藏
页码:3373 / 3383
页数:11
相关论文
共 60 条
[1]   Fission yeast homolog of murine int-6 protein, encoded by mouse mammary tumor virus integration site, is associated with the conserved core subunits of eukaryotic translation initiation factor 3 [J].
Akiyoshi, Y ;
Clayton, J ;
Phan, L ;
Yamamoto, M ;
Hinnebusch, AG ;
Watanabe, Y ;
Asano, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (13) :10056-10062
[2]   In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3 [J].
Alkalaeva, Elena Z. ;
Pisarev, Andrey V. ;
Frolova, Lyudmila Y. ;
Kisselev, Lev L. ;
Pestova, Tatyana V. .
CELL, 2006, 125 (06) :1125-1136
[3]   Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae [J].
Asano, K ;
Phan, L ;
Anderson, J ;
Hinnebusch, AG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (29) :18573-18585
[4]   Conservation and diversity of eukaryotic translation initiation factor eIF3 [J].
Asano, K ;
Kinzy, TG ;
Merrick, WC ;
Hershey, JWB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (02) :1101-1109
[5]   The translation initiation factor eIF3-p48 subunit is encoded by int-6, a site of frequent integration by the mouse mammary tumor virus genome [J].
Asano, K ;
Merrick, WC ;
Hershey, JWB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (38) :23477-23480
[6]   Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits - Possible roles in RNA binding and macromolecular assembly [J].
Asano, K ;
Vornlocher, HP ;
RichterCook, NJ ;
Merrick, WC ;
Hinnebusch, AG ;
Hershey, JWB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (43) :27042-27052
[7]   Fission yeast int6 is not essential for global translation initiation, but deletion of int6+ causes hypersensitivity to caffeine and affects spore formation [J].
Bandyopadhyay, A ;
Matsumoto, T ;
Maitra, U .
MOLECULAR BIOLOGY OF THE CELL, 2000, 11 (11) :4005-4018
[8]   Moe1 and spInt6, the fission yeast homologues of mammalian translation initiation factor 3 Subunits p66 (eIF3d) and p48 (eIF3e), respectively, are required for stable association of eIF3 Subunits [J].
Bandyopadhyay, A ;
Lakshmanan, V ;
Matsumoto, T ;
Chang, EC ;
Maitra, U .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (03) :2360-2367
[9]   20S proteasome differentially alters translation of different mRNAs via the cleavage of elF4F and elF3 [J].
Baugh, JM ;
Pilipenko, EV .
MOLECULAR CELL, 2004, 16 (04) :575-586
[10]   STRUCTURE OF INITIATION-FACTOR EIF-3 FROM RAT-LIVER - HYDRODYNAMIC AND ELECTRON-MICROSCOPIC INVESTIGATIONS [J].
BEHLKE, J ;
BOMMER, UA ;
LUTSCH, G ;
HENSKE, A ;
BIELKA, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1986, 157 (03) :523-530